Chlorine in PDB 6dxx: Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100

Enzymatic activity of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100

All present enzymatic activity of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100:
3.5.1.60;

Protein crystallography data

The structure of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100, PDB code: 6dxx was solved by A.Gorelik, A.Gebai, K.Illes, D.Piomelli, B.Nagar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.11 / 2.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 76.610, 99.798, 92.756, 90.00, 96.13, 90.00
R / Rfree (%) 20.6 / 24.6

Other elements in 6dxx:

The structure of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Chlorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Chlorine atom in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 (pdb code 6dxx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 12 binding sites of Chlorine where determined in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100, PDB code: 6dxx:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 12 in 6dxx

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Chlorine binding site 1 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl204

b:50.8
occ:1.00
 HA A:SER123 3.3 63.3 1.0
HD21 B:ASN204 3.5 48.6 1.0
HB2 A:SER123 3.6 62.9 1.0
O A:TYR120 3.7 39.1 1.0
HB3 A:SER123 3.8 62.9 1.0
HB1 B:ALA244 3.9 41.0 1.0
OD1 B:ASP197 4.0 64.0 1.0
CB A:SER123 4.0 51.9 1.0
CA A:SER123 4.1 52.3 1.0
HA B:ASP197 4.1 50.4 1.0
O A:HOH309 4.2 55.4 1.0
ND2 B:ASN204 4.2 40.0 1.0
HD22 B:ASN204 4.4 48.6 1.0
CZ A:TYR120 4.4 28.1 1.0
CE1 A:TYR120 4.5 30.6 1.0
HB2 B:ALA244 4.6 41.0 1.0
HE1 A:TYR120 4.7 37.2 1.0
OH A:TYR120 4.7 38.6 1.0
CB B:ALA244 4.7 33.7 1.0
O B:ARG196 4.7 38.9 1.0
CE2 A:TYR120 4.7 29.1 1.0
H A:SER123 4.7 49.1 1.0
HG3 B:GLU195 4.8 41.9 1.0
HH A:TYR120 4.8 46.9 1.0
CG B:ASP197 4.8 61.6 1.0
H B:LYS198 4.9 54.5 1.0
N A:SER123 4.9 40.5 1.0
CD1 A:TYR120 4.9 36.4 1.0
C A:TYR120 4.9 32.8 1.0
HB3 B:ALA244 5.0 41.0 1.0

Chlorine binding site 2 out of 12 in 6dxx

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Chlorine binding site 2 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl402

b:37.7
occ:1.00
 HE B:ARG221 2.9 43.9 1.0
HG B:SER225 3.2 49.1 1.0
HH21 B:ARG221 3.3 42.5 1.0
HB2 B:SER225 3.3 52.6 1.0
HZ B:PHE169 3.4 43.6 1.0
HG2 B:ARG221 3.5 47.4 1.0
O A:HOH321 3.6 32.1 1.0
NE B:ARG221 3.6 36.1 1.0
HB3 B:SER225 3.8 52.6 1.0
CB B:SER225 3.8 43.4 1.0
OG B:SER225 3.8 40.5 1.0
HD13 A:LEU40 3.9 45.2 1.0
NH2 B:ARG221 3.9 34.9 1.0
HD11 A:LEU40 4.0 45.2 1.0
HD22 A:LEU40 4.1 54.0 1.0
CZ B:ARG221 4.2 32.7 1.0
CZ B:PHE169 4.2 35.9 1.0
HD21 A:LEU40 4.2 54.0 1.0
HE2 B:PHE169 4.3 43.1 1.0
HG3 A:PRO94 4.4 68.9 1.0
CG B:ARG221 4.4 39.0 1.0
CD1 A:LEU40 4.4 37.2 1.0
HA B:ALA222 4.5 38.2 1.0
HG2 A:PRO94 4.5 68.9 1.0
CD B:ARG221 4.6 36.1 1.0
CD2 A:LEU40 4.6 44.5 1.0
CE2 B:PHE169 4.6 35.5 1.0
HH22 B:ARG221 4.6 42.5 1.0
O B:ARG221 4.7 30.7 1.0
HH12 A:ARG47 4.7 76.7 1.0
HZ A:PHE95 4.7 63.4 1.0
HD2 A:PRO94 4.8 61.3 1.0
HG3 B:ARG221 4.8 47.4 1.0
CG A:PRO94 4.8 56.9 1.0
HD3 B:ARG221 4.9 43.9 1.0

Chlorine binding site 3 out of 12 in 6dxx

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Chlorine binding site 3 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl403

b:50.2
occ:1.00
 H B:VAL284 2.8 35.5 1.0
HH2 B:TRP272 2.9 45.1 1.0
HE1 B:PHE282 3.2 36.0 1.0
HA B:ARG283 3.3 40.9 1.0
HD11 B:ILE305 3.4 48.7 1.0
HB B:VAL284 3.5 35.1 1.0
HD13 B:ILE305 3.5 48.7 1.0
CH2 B:TRP272 3.6 37.1 1.0
O B:HOH557 3.6 37.0 1.0
N B:VAL284 3.6 29.1 1.0
HD1 B:PHE282 3.7 35.0 1.0
HG12 B:ILE305 3.8 44.8 1.0
HG23 B:VAL284 3.8 40.1 1.0
CD1 B:ILE305 3.9 40.1 1.0
CE1 B:PHE282 4.0 29.5 1.0
HH11 B:ARG283 4.0 46.5 1.0
HZ3 B:TRP272 4.1 41.0 1.0
HD3 B:ARG283 4.1 45.2 1.0
CA B:ARG283 4.2 33.6 1.0
CD1 B:PHE282 4.2 28.7 1.0
CZ3 B:TRP272 4.2 33.7 1.0
CB B:VAL284 4.2 28.8 1.0
O B:PHE282 4.3 37.5 1.0
C B:ARG283 4.3 27.3 1.0
HD2 B:ARG283 4.4 45.2 1.0
CZ2 B:TRP272 4.4 41.3 1.0
HZ2 B:TRP272 4.4 50.1 1.0
CG1 B:ILE305 4.4 36.9 1.0
O B:VAL284 4.4 27.7 1.0
CA B:VAL284 4.4 22.2 1.0
CG2 B:VAL284 4.4 33.0 1.0
HG21 B:VAL284 4.7 40.1 1.0
CD B:ARG283 4.7 37.2 1.0
HD12 B:ILE305 4.8 48.7 1.0
HG23 B:ILE305 4.8 40.8 1.0
NH1 B:ARG283 4.8 38.3 1.0
HD3 B:ARG301 4.8 52.8 1.0
HG13 B:ILE305 4.9 44.8 1.0
C B:VAL284 4.9 20.9 1.0
C B:PHE282 4.9 34.2 1.0
HB3 B:ARG283 5.0 32.8 1.0
N B:ARG283 5.0 38.9 1.0

Chlorine binding site 4 out of 12 in 6dxx

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Chlorine binding site 4 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl202

b:69.7
occ:1.00
 HH21 C:ARG47 3.3 60.8 1.0
HA C:VAL43 3.9 45.8 1.0
O C:ASP41 3.9 51.2 1.0
NH2 C:ARG47 4.0 50.2 1.0
HD3 C:PRO44 4.0 58.5 1.0
O C:LEU40 4.0 36.6 1.0
HH22 C:ARG47 4.1 60.8 1.0
O C:SER42 4.1 41.2 1.0
HA C:ASP41 4.3 54.2 1.0
C C:ASP41 4.5 46.1 1.0
C C:SER42 4.5 36.4 1.0
CA C:VAL43 4.7 37.7 1.0
HG22 C:VAL43 4.8 59.0 1.0
N C:VAL43 4.9 40.9 1.0
CA C:ASP41 4.9 44.7 1.0
HE C:ARG47 4.9 44.1 1.0
CD C:PRO44 4.9 48.3 1.0

Chlorine binding site 5 out of 12 in 6dxx

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Chlorine binding site 5 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl203

b:38.8
occ:1.00
 HD3 C:ARG53 2.6 76.9 1.0
HA C:PRO50 3.3 29.8 1.0
CD C:ARG53 3.4 63.6 1.0
HD2 C:ARG53 3.4 76.9 1.0
HG3 C:ARG53 3.6 70.1 1.0
HB3 C:LEU49 3.7 40.2 1.0
HB2 C:LEU49 3.8 40.2 1.0
HG3 C:PRO50 3.8 39.8 1.0
N C:PRO50 3.9 28.7 1.0
C C:LEU49 4.0 30.1 1.0
CA C:PRO50 4.0 24.4 1.0
CG C:ARG53 4.1 58.0 1.0
O C:LEU49 4.1 30.9 1.0
HD3 C:PRO50 4.1 39.7 1.0
CB C:LEU49 4.1 33.0 1.0
CD C:PRO50 4.4 32.6 1.0
CG C:PRO50 4.4 32.7 1.0
HB2 C:ARG53 4.5 50.5 1.0
NE C:ARG53 4.5 54.0 1.0
HE C:ARG53 4.6 65.3 1.0
HB3 C:PRO50 4.7 37.6 1.0
CB C:PRO50 4.7 30.9 1.0
CA C:LEU49 4.7 31.3 1.0
HG2 C:ARG53 4.8 70.1 1.0
CB C:ARG53 4.9 41.6 1.0

Chlorine binding site 6 out of 12 in 6dxx

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Chlorine binding site 6 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl204

b:66.0
occ:1.00
 HB2 C:SER123 3.0 93.0 1.0
HA C:SER123 3.1 78.5 1.0
HB3 C:SER123 3.3 93.0 1.0
CB C:SER123 3.5 77.0 1.0
O D:HOH537 3.5 53.2 1.0
HD21 D:ASN204 3.6 53.9 1.0
O C:TYR120 3.7 34.9 1.0
CA C:SER123 3.8 65.0 1.0
OD1 D:ASP197 3.8 68.3 1.0
HA D:ASP197 4.2 60.3 1.0
HB1 D:ALA244 4.3 38.5 1.0
ND2 D:ASN204 4.4 44.5 1.0
HD22 D:ASN204 4.5 53.9 1.0
OE2 D:GLU195 4.6 57.3 1.0
H C:SER123 4.6 71.6 1.0
N C:SER123 4.7 59.2 1.0
HG3 D:GLU195 4.7 57.4 1.0
O C:SER123 4.7 66.5 1.0
C C:SER123 4.8 65.8 1.0
OG C:SER123 4.8 68.4 1.0
CZ C:TYR120 4.9 34.7 1.0
HB2 D:ALA244 4.9 38.5 1.0
C C:TYR120 4.9 29.7 1.0
CG D:ASP197 5.0 65.2 1.0
O D:ARG196 5.0 37.3 1.0

Chlorine binding site 7 out of 12 in 6dxx

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Chlorine binding site 7 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl402

b:51.6
occ:1.00
 HH2 D:TRP272 2.9 55.0 1.0
HA D:ARG283 3.0 44.6 1.0
H D:VAL284 3.1 45.0 1.0
HE1 D:PHE282 3.3 45.7 1.0
HH11 D:ARG283 3.4 60.3 1.0
CH2 D:TRP272 3.5 45.4 1.0
HD1 D:PHE282 3.5 43.6 1.0
HD3 D:ARG283 3.6 38.9 1.0
O D:PHE282 3.7 45.0 1.0
HD13 D:ILE305 3.8 63.8 1.0
N D:VAL284 3.8 37.1 1.0
CE1 D:PHE282 3.9 37.6 1.0
CA D:ARG283 4.0 36.7 1.0
HD2 D:ARG283 4.0 38.9 1.0
CD1 D:PHE282 4.0 35.9 1.0
HD11 D:ILE305 4.0 63.8 1.0
HZ2 D:TRP272 4.1 46.1 1.0
HB D:VAL284 4.1 45.4 1.0
HG23 D:VAL284 4.1 45.4 1.0
CZ2 D:TRP272 4.1 38.0 1.0
HG12 D:ILE305 4.2 58.7 1.0
HZ3 D:TRP272 4.2 49.0 1.0
CZ3 D:TRP272 4.2 40.3 1.0
CD D:ARG283 4.3 32.0 1.0
NH1 D:ARG283 4.3 49.8 1.0
CD1 D:ILE305 4.3 52.7 1.0
C D:ARG283 4.4 34.1 1.0
C D:PHE282 4.5 37.4 1.0
HH12 D:ARG283 4.6 60.3 1.0
N D:ARG283 4.7 36.5 1.0
HG23 D:ILE305 4.7 59.4 1.0
CB D:VAL284 4.8 37.4 1.0
CG1 D:ILE305 4.8 48.4 1.0
HB3 D:ARG283 4.8 44.8 1.0
CA D:VAL284 4.9 33.1 1.0
CG2 D:VAL284 4.9 37.4 1.0
CB D:ARG283 4.9 36.9 1.0
HG21 D:ILE305 5.0 59.4 1.0
O D:VAL284 5.0 45.5 1.0

Chlorine binding site 8 out of 12 in 6dxx

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Chlorine binding site 8 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl403

b:61.1
occ:1.00
 HZ1 D:LYS188 3.1 80.2 1.0
HZ3 D:LYS188 3.2 80.2 1.0
HZ2 D:LYS188 3.2 80.2 1.0
NZ D:LYS188 3.4 66.4 1.0
O D:GLU226 3.8 30.8 1.0
O D:SER225 3.8 41.8 1.0
OE1 D:GLU228 3.9 82.2 1.0
HA D:GLU226 4.2 45.9 1.0
HA D:GLU228 4.2 55.9 1.0
CD D:GLU228 4.3 70.9 1.0
OE2 D:GLU228 4.4 63.2 1.0
C D:GLU226 4.5 24.9 1.0
O D:SER227 4.6 43.1 1.0
HZ3 D:LYS163 4.7 50.1 1.0
O D:HOH514 4.8 43.2 1.0
CA D:GLU226 4.8 37.8 1.0
HZ2 D:LYS163 4.8 50.1 1.0
CE D:LYS188 4.8 54.7 1.0
C D:SER225 4.9 33.9 1.0

Chlorine binding site 9 out of 12 in 6dxx

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Chlorine binding site 9 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl404

b:64.5
occ:1.00
 HD2 D:TYR349 2.3 39.6 1.0
HH22 C:ARG35 2.4 93.7 1.0
OD2 D:ASP158 2.6 35.7 1.0
NH2 C:ARG35 2.7 77.7 1.0
HH12 C:ARG35 3.1 0.5 1.0
HH21 C:ARG35 3.1 93.7 1.0
CD2 D:TYR349 3.2 32.5 1.0
HB3 D:ASP158 3.2 41.7 1.0
CZ C:ARG35 3.2 90.2 1.0
CG D:ASP158 3.2 31.1 1.0
O D:HOH502 3.2 33.9 1.0
NH1 C:ARG35 3.3 83.3 1.0
O D:TYR349 3.5 41.2 1.0
CB D:ASP158 3.5 34.3 1.0
HE2 D:TYR349 3.5 42.7 1.0
HB2 D:ASP158 3.6 41.7 1.0
HA D:MET350 3.7 45.6 1.0
HB3 D:TYR349 3.7 43.9 1.0
CE2 D:TYR349 3.8 35.1 1.0
H D:THR351 3.9 50.8 1.0
C D:TYR349 3.9 34.5 1.0
HH11 C:ARG35 4.0 0.5 1.0
OD1 D:ASP158 4.1 37.0 1.0
HG21 D:THR170 4.1 38.1 1.0
NE C:ARG35 4.1 99.7 1.0
CG D:TYR349 4.1 32.0 1.0
N D:MET350 4.3 35.4 1.0
CA D:MET350 4.3 37.5 1.0
CB D:TYR349 4.3 36.1 1.0
HE C:ARG35 4.4 0.2 1.0
N D:THR351 4.4 41.8 1.0
HG3 C:ARG35 4.5 80.3 1.0
OG1 D:THR351 4.5 41.9 1.0
HB D:THR351 4.6 42.3 1.0
HG1 D:THR351 4.7 50.9 1.0
C D:MET350 4.7 37.7 1.0
H D:MET350 4.8 43.0 1.0
CA D:TYR349 4.8 34.2 1.0
HB2 C:ARG35 4.9 55.9 1.0
CG2 D:THR170 4.9 31.3 1.0

Chlorine binding site 10 out of 12 in 6dxx

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Chlorine binding site 10 out of 12 in the Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Human N-Acylethanolamine-Hydrolyzing Acid Amidase (Naaa) in Complex with Non-Covalent Benzothiazole-Piperazine Inhibitor ARN19702, in Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl405

b:68.3
occ:1.00
 HE1 D:HIS213 2.5 59.5 1.0
HB3 D:ASP266 2.6 55.4 1.0
HH11 D:ARG211 2.7 98.0 1.0
HH12 D:ARG211 3.0 98.0 1.0
NH1 D:ARG211 3.0 81.2 1.0
CE1 D:HIS213 3.4 49.1 1.0
CB D:ASP266 3.5 45.7 1.0
HB2 D:ARG265 3.6 40.7 1.0
HA D:ASP266 3.6 47.3 1.0
HD3 D:ARG211 3.7 92.3 1.0
N D:ASP266 3.8 43.7 1.0
HB3 D:ARG265 3.8 40.7 1.0
CA D:ASP266 3.9 39.0 1.0
H D:ASP266 3.9 53.0 1.0
HB2 D:ASP266 4.0 55.4 1.0
CZ D:ARG211 4.1 77.6 1.0
CB D:ARG265 4.1 33.5 1.0
C D:ARG265 4.2 39.7 1.0
NE2 D:HIS213 4.3 54.7 1.0
ND1 D:HIS213 4.3 43.9 1.0
HD1 D:HIS213 4.3 53.3 1.0
CG D:ASP266 4.5 59.3 1.0
CD D:ARG211 4.5 76.5 1.0
HD2 D:ARG211 4.6 92.3 1.0
O D:ARG265 4.6 39.1 1.0
NE D:ARG211 4.6 77.3 1.0
CA D:ARG265 4.8 36.9 1.0
OD1 D:ASP266 4.8 54.2 1.0
HB2 D:ALA207 4.9 58.0 1.0
HH22 D:ARG211 4.9 75.6 1.0
NH2 D:ARG211 5.0 62.5 1.0

Reference:

A.Gorelik, A.Gebai, K.Illes, D.Piomelli, B.Nagar. Molecular Mechanism of Activation of the Immunoregulatory Amidase Naaa. Proc. Natl. Acad. Sci. V. 115 10032 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30301806
DOI: 10.1073/PNAS.1811759115
Page generated: Sat Dec 12 12:54:06 2020

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