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Chlorine in PDB 6o07: Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex

Enzymatic activity of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex

All present enzymatic activity of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex:
2.3.1.255; 2.3.1.258;

Protein crystallography data

The structure of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex, PDB code: 6o07 was solved by S.Deng, R.Marmorstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.66 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.437, 125.726, 145.924, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 25

Chlorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 18;

Binding sites:

The binding sites of Chlorine atom in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex (pdb code 6o07). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 18 binding sites of Chlorine where determined in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex, PDB code: 6o07:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 18 in 6o07

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Chlorine binding site 1 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl201

b:0.3
occ:1.00
 OE1 C:GLN166 2.9 0.6 1.0
O C:ASP167 3.4 0.9 1.0
CB C:PRO132 3.9 99.3 1.0
N C:ASP167 3.9 0.6 1.0
N C:ALA133 4.1 97.8 1.0
CD C:GLN166 4.1 0.8 1.0
N C:VAL134 4.2 94.6 1.0
C C:GLN166 4.3 0.8 1.0
C C:ASP167 4.3 0.8 1.0
CB C:VAL134 4.4 91.4 1.0
CA C:GLN166 4.4 1.0 1.0
CA C:ASP167 4.5 0.5 1.0
CA C:PRO132 4.5 97.3 1.0
CB C:GLN166 4.5 0.4 1.0
CB C:ASP167 4.6 0.7 1.0
C C:PRO132 4.7 99.3 1.0
CG C:GLN166 4.8 0.3 1.0
CA C:ALA133 4.9 92.7 1.0
CA C:VAL134 5.0 97.3 1.0

Chlorine binding site 2 out of 18 in 6o07

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Chlorine binding site 2 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl901

b:69.8
occ:1.00
 CE A:LYS515 3.4 49.0 1.0
OH A:TYR511 3.5 51.8 1.0
NZ A:LYS551 3.8 46.8 1.0
CE1 A:TYR511 4.0 45.9 1.0
CZ A:TYR511 4.2 47.1 1.0
CD A:LYS515 4.3 53.0 1.0
CG1 A:VAL547 4.5 52.0 1.0
NZ A:LYS515 4.5 55.4 1.0
CG A:LYS515 4.7 58.1 1.0
CD A:LYS551 4.7 40.8 1.0
CE A:LYS551 4.7 50.5 1.0
NE2 A:GLN617 5.0 62.7 1.0

Chlorine binding site 3 out of 18 in 6o07

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Chlorine binding site 3 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl902

b:77.7
occ:1.00
 CG A:GLN617 3.3 55.4 1.0
CB A:GLN617 3.5 42.4 1.0
CA A:GLN617 3.6 44.5 1.0
CB A:ASP620 4.0 50.7 1.0
O A:GLN617 4.2 54.5 1.0
C A:GLN617 4.4 48.1 1.0
OD1 A:ASP621 4.4 73.2 1.0
OD2 A:ASP620 4.5 58.8 1.0
OD2 A:ASP621 4.6 69.4 1.0
CG A:ASP621 4.6 69.5 1.0
CD A:GLN617 4.6 61.5 1.0
N A:GLN617 4.7 45.6 1.0
CG A:ASP620 4.7 49.2 1.0
NE2 A:GLN617 4.9 62.7 1.0

Chlorine binding site 4 out of 18 in 6o07

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Chlorine binding site 4 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl903

b:78.0
occ:1.00
 OE2 A:GLU693 3.6 62.7 1.0
CB A:ALA696 3.8 43.7 1.0
OE1 A:GLU693 3.8 66.1 1.0
OD1 A:ASN701 4.1 46.2 1.0
CZ A:PHE720 4.1 32.1 1.0
CD A:GLU693 4.1 69.6 1.0
O A:HOH1132 4.4 42.0 1.0
CE2 A:PHE720 4.5 30.4 1.0
ND2 A:ASN701 4.6 42.2 1.0
CG A:ASN701 4.8 41.1 1.0
CD1 A:ILE724 4.9 33.9 1.0

Chlorine binding site 5 out of 18 in 6o07

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Chlorine binding site 5 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl904

b:0.3
occ:1.00
 CL A:CL905 4.2 94.6 1.0

Chlorine binding site 6 out of 18 in 6o07

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Chlorine binding site 6 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl905

b:94.6
occ:1.00
 CL A:CL904 4.2 0.3 1.0

Chlorine binding site 7 out of 18 in 6o07

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Chlorine binding site 7 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl906

b:65.3
occ:1.00
 OE1 A:GLU443 3.7 48.3 1.0
NZ C:LYS21 4.1 47.0 1.0
CE2 A:TYR421 4.1 45.1 1.0
OH A:TYR421 4.2 53.9 1.0
CZ A:TYR421 4.4 49.4 1.0
CE C:LYS21 4.5 54.0 1.0
CD2 A:LEU411 4.5 46.0 1.0
CD1 A:LEU411 4.7 51.5 1.0
CD A:GLU443 4.8 48.0 1.0
CD2 A:TYR421 5.0 42.7 1.0

Chlorine binding site 8 out of 18 in 6o07

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Chlorine binding site 8 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl907

b:79.5
occ:1.00
 CD1 A:LEU257 4.0 41.6 1.0
CA A:GLY286 4.3 59.7 1.0
NE2 A:GLN288 4.6 65.5 1.0

Chlorine binding site 9 out of 18 in 6o07

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Chlorine binding site 9 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl908

b:75.3
occ:1.00
 OG A:SER612 2.7 39.0 1.0
CE A:LYS609 3.7 44.9 1.0
NZ A:LYS609 3.8 41.9 1.0
O A:LYS609 3.9 37.1 1.0
CD A:LYS609 4.0 45.2 1.0
CB A:SER612 4.0 36.4 1.0
OE1 A:GLU719 4.4 58.5 1.0
CE2 A:PHE616 4.5 40.1 1.0
CG A:LYS613 4.6 26.4 1.0
CD1 A:LEU716 4.6 36.0 1.0
CD2 A:PHE616 4.6 37.7 1.0
CG A:LYS609 4.7 34.1 1.0
N A:LYS613 4.7 40.7 1.0
C A:SER612 4.9 43.4 1.0
C A:LYS609 4.9 36.7 1.0

Chlorine binding site 10 out of 18 in 6o07

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Chlorine binding site 10 out of 18 in the Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl909

b:65.1
occ:1.00
 O A:TYR722 3.4 38.0 1.0
O A:HOH1116 3.9 43.0 1.0
CE1 A:HIS619 3.9 45.5 1.0
NE2 A:HIS619 4.0 45.6 1.0
CA A:ARG723 4.0 40.3 1.0
C A:ARG723 4.2 42.2 1.0
O A:ARG723 4.2 47.3 1.0
CE1 A:PHE765 4.3 45.3 1.0
C A:TYR722 4.4 39.0 1.0
CZ A:PHE765 4.5 41.8 1.0
CD1 A:LEU623 4.7 56.3 1.0
N A:ARG723 4.7 43.1 1.0
N A:ILE724 4.9 39.2 1.0

Reference:

S.Deng, R.S.Magin, X.Wei, B.Pan, E.J.Petersson, R.Marmorstein. Structure and Mechanism of Acetylation By the N-Terminal Dual Enzyme Nata/NAA50 Complex. Structure V. 27 1057 2019.
ISSN: ISSN 0969-2126
PubMed: 31155310
DOI: 10.1016/J.STR.2019.04.014
Page generated: Mon Jul 29 12:22:13 2024

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