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Chlorine in PDB 5mrr: Crystal Structure of L1 Protease of Lysobacter Sp. XL1

Protein crystallography data

The structure of Crystal Structure of L1 Protease of Lysobacter Sp. XL1, PDB code: 5mrr was solved by A.Gabdulkhakov, S.Tishchenko, A.Lisov, A.Leontievsky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.99 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.710, 96.480, 118.180, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 19

Other elements in 5mrr:

The structure of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 also contains other interesting chemical elements:

Sodium (Na) 1 atom

Chlorine Binding Sites:

Pages:

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

Binding sites:

The binding sites of Chlorine atom in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1 (pdb code 5mrr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 11 binding sites of Chlorine where determined in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1, PDB code: 5mrr:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 11 in 5mrr

Go back to Chlorine Binding Sites List in 5mrr
Chlorine binding site 1 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:30.4
occ:1.00
O A:HOH347 2.6 31.3 1.0
O A:HOH461 2.8 33.9 1.0
N A:ILE97 3.2 10.6 1.0
NZ A:LYS118 3.6 15.0 1.0
CA A:ALA96 3.6 12.0 1.0
CG1 A:ILE97 3.7 15.2 0.5
CE A:LYS118 3.7 13.3 1.0
CG2 A:ILE97 3.7 12.9 0.5
CB A:ALA96 3.8 13.0 1.0
C A:ALA96 3.9 10.5 1.0
CG1 A:ILE97 3.9 13.3 0.5
CD A:LYS118 3.9 13.2 1.0
CB A:ILE97 4.0 13.7 0.5
CB A:ILE97 4.1 13.1 0.5
CA A:ILE97 4.2 11.8 0.5
CA A:ILE97 4.2 11.6 0.5
CD1 A:ILE97 4.5 16.5 0.5
O A:HOH426 4.5 30.3 1.0
CG A:LYS118 4.7 12.2 1.0
CD1 A:ILE97 4.8 14.6 0.5
O A:HOH394 4.9 17.6 1.0
N A:ALA96 5.0 10.8 1.0

Chlorine binding site 2 out of 11 in 5mrr

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Chlorine binding site 2 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl203

b:30.9
occ:1.00
O A:HOH367 2.7 22.1 1.0
N A:GLY186 2.8 9.8 1.0
O A:HOH352 3.2 13.8 1.0
CA A:GLY186 3.4 10.7 1.0
N A:VAL185 3.6 7.9 1.0
CB A:ARG184 3.7 9.7 0.5
CB A:ARG184 3.7 10.2 0.5
C A:VAL185 3.9 8.9 1.0
OE1 A:GLU94 4.0 17.1 1.0
CG1 A:VAL185 4.0 12.1 1.0
C A:ARG184 4.0 8.9 1.0
CD A:PRO187 4.0 11.5 1.0
O A:GLN156 4.1 8.5 1.0
NE A:ARG184 4.1 14.8 0.5
NH2 A:ARG184 4.2 17.1 0.5
CA A:VAL185 4.2 9.0 1.0
CA A:ARG184 4.2 9.2 0.5
CA A:ARG184 4.2 9.3 0.5
NH1 A:ARG184 4.3 17.3 0.5
CZ A:ARG184 4.4 16.4 0.5
CG A:ARG184 4.5 11.5 0.5
O A:HOH447 4.5 35.7 1.0
CD A:GLU94 4.5 16.3 1.0
CG A:ARG184 4.5 10.8 0.5
CB A:GLU94 4.6 11.6 1.0
CD A:ARG184 4.6 12.1 0.5
C A:GLY186 4.6 10.7 1.0
O A:HOH337 4.7 32.2 1.0
CB A:VAL185 4.7 10.3 1.0
O A:SER92 4.7 12.3 1.0
N A:PRO187 4.8 10.7 1.0
CG A:GLU94 4.8 13.7 1.0
O A:ARG184 4.8 9.9 1.0
CD A:ARG184 4.9 13.1 0.5
CZ A:ARG184 5.0 15.8 0.5

Chlorine binding site 3 out of 11 in 5mrr

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Chlorine binding site 3 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl204

b:33.0
occ:1.00
N A:LEU75 2.9 13.1 1.0
NZ A:LYS29 3.1 17.0 1.0
CA A:THR74 3.5 14.9 0.4
CA A:THR74 3.5 15.0 0.6
CE A:LYS29 3.6 14.4 1.0
C A:THR74 3.7 14.2 0.4
C A:THR74 3.7 14.6 0.6
O A:HIS73 3.7 18.0 1.0
O A:HOH359 3.8 32.0 1.0
CB A:LEU75 3.9 11.4 1.0
CA A:LEU75 4.0 11.1 1.0
CD A:LYS29 4.0 12.4 1.0
CG A:LEU75 4.0 11.9 1.0
CG2 A:THR74 4.1 15.2 0.6
O A:LEU75 4.2 14.4 1.0
CB A:THR74 4.3 16.0 0.4
CB A:THR74 4.3 15.8 0.6
N A:THR74 4.5 14.2 0.6
N A:THR74 4.5 14.3 0.4
C A:HIS73 4.5 15.0 1.0
C A:LEU75 4.6 12.4 1.0
CG2 A:THR74 4.6 16.6 0.4
CD1 A:LEU75 4.8 12.4 1.0
OG1 A:THR74 4.8 17.3 0.6
CG A:LYS29 4.9 11.9 1.0
O A:THR74 4.9 14.8 0.4
O A:THR74 4.9 16.4 0.6

Chlorine binding site 4 out of 11 in 5mrr

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Chlorine binding site 4 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl205

b:47.3
occ:1.00
N A:ALA125 3.4 16.7 1.0
CA A:TYR124 4.0 14.4 1.0
CB A:ALA125 4.0 18.8 1.0
O A:HOH407 4.0 24.8 1.0
CB A:TYR124 4.2 14.3 1.0
C A:TYR124 4.2 14.6 1.0
CD1 A:TYR124 4.3 12.4 1.0
CA A:ALA125 4.3 17.1 1.0
CG A:TYR124 4.7 12.8 1.0

Chlorine binding site 5 out of 11 in 5mrr

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Chlorine binding site 5 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl203

b:33.1
occ:1.00
N B:ILE97 3.2 9.1 1.0
NZ B:LYS118 3.4 17.7 1.0
CG1 B:ILE97 3.6 12.9 1.0
CE B:LYS118 3.7 15.4 1.0
CA B:ALA96 3.7 10.4 1.0
C B:ALA96 3.9 8.7 1.0
CD B:LYS118 3.9 15.5 1.0
CB B:ALA96 3.9 11.6 1.0
CB B:ILE97 3.9 11.6 1.0
CD1 B:ILE97 4.0 15.7 1.0
CA B:ILE97 4.2 9.1 1.0
O B:HOH356 4.3 14.3 1.0
O B:HOH389 4.4 31.4 1.0
CG B:LYS118 4.7 13.6 1.0
O B:ALA95 4.9 11.1 1.0
N B:ALA96 5.0 10.6 1.0

Chlorine binding site 6 out of 11 in 5mrr

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Chlorine binding site 6 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl204

b:31.9
occ:1.00
O B:HOH324 3.0 22.4 1.0
ND2 B:ASN12 3.1 13.9 1.0
O C:ARG57 3.3 11.6 1.0
N C:ARG57 3.3 10.1 1.0
CB B:ASN12 3.3 13.2 1.0
O B:HOH316 3.4 25.8 1.0
CG B:ASN12 3.7 14.2 1.0
CA C:ALA56 3.9 10.4 1.0
CB C:VAL40 4.0 13.8 1.0
CG C:ARG57 4.1 17.1 1.0
C C:ALA56 4.1 9.8 1.0
C C:ARG57 4.1 10.5 1.0
O C:HOH358 4.2 15.0 1.0
CA C:ARG57 4.2 10.4 1.0
CB C:ALA56 4.5 10.8 1.0
CG1 C:VAL40 4.5 15.2 1.0
CG2 C:VAL40 4.6 14.3 1.0
O B:ASN12 4.6 15.6 1.0
CB C:ARG57 4.7 12.8 1.0
CA B:ASN12 4.7 14.0 1.0
O B:ILE11 4.7 12.5 1.0
CB B:ALA14 4.7 16.9 1.0
OD1 B:ASN12 4.9 14.6 1.0
N C:VAL40 4.9 11.8 1.0
CA C:VAL40 4.9 12.3 1.0

Chlorine binding site 7 out of 11 in 5mrr

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Chlorine binding site 7 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl205

b:46.3
occ:1.00
N B:SER71 3.4 21.1 1.0
OG B:SER71 3.5 28.6 1.0
CB B:SER71 3.8 25.5 1.0
CA B:GLY70 4.1 16.7 1.0
CA B:SER71 4.2 23.3 1.0
C B:GLY70 4.2 18.5 1.0
O B:HOH424 4.3 26.2 1.0
O B:HOH325 4.5 18.0 1.0

Chlorine binding site 8 out of 11 in 5mrr

Go back to Chlorine Binding Sites List in 5mrr
Chlorine binding site 8 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl203

b:34.3
occ:1.00
O C:HOH443 2.8 33.7 1.0
N C:ALA96 3.0 13.0 1.0
CA C:ALA95 3.5 12.8 1.0
C C:ALA95 3.7 13.3 1.0
CB C:ALA96 3.8 14.7 1.0
CB C:ALA95 3.9 13.6 1.0
CB C:ALA99 3.9 11.6 1.0
CA C:ALA96 3.9 13.4 1.0
O C:HOH444 4.5 36.7 1.0
O C:ALA96 4.6 11.6 1.0
O C:GLU94 4.7 15.6 1.0
C C:ALA96 4.7 11.3 1.0
N C:ALA95 4.8 10.9 1.0
O C:HOH397 4.8 22.7 1.0
O C:HOH370 4.9 24.4 1.0
O C:ALA95 4.9 14.4 1.0

Chlorine binding site 9 out of 11 in 5mrr

Go back to Chlorine Binding Sites List in 5mrr
Chlorine binding site 9 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl204

b:43.0
occ:1.00
O C:HOH332 2.8 39.6 1.0
N C:ALA125 3.3 14.0 1.0
O A:HOH388 3.5 23.6 1.0
CA C:TYR124 3.8 11.5 1.0
CB C:ALA125 4.0 17.5 1.0
C C:TYR124 4.1 12.7 1.0
CA A:GLY84 4.1 17.9 1.0
CB C:TYR124 4.2 11.9 1.0
CD1 C:TYR124 4.2 10.7 1.0
CA C:ALA125 4.3 16.9 1.0
O C:HOH404 4.3 33.3 1.0
O2 C:GOL207 4.4 31.5 1.0
N A:GLY84 4.6 18.2 1.0
CG C:TYR124 4.6 10.9 1.0
O1 C:GOL207 4.9 33.6 1.0
O A:HOH336 4.9 17.4 1.0
O C:ASN123 5.0 16.7 1.0

Chlorine binding site 10 out of 11 in 5mrr

Go back to Chlorine Binding Sites List in 5mrr
Chlorine binding site 10 out of 11 in the Crystal Structure of L1 Protease of Lysobacter Sp. XL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Crystal Structure of L1 Protease of Lysobacter Sp. XL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl202

b:26.4
occ:1.00
O D:HOH388 2.7 30.4 1.0
N D:TYR110 2.9 8.8 1.0
NA D:NA204 3.0 22.7 1.0
CB D:TYR82 3.5 10.4 1.0
CA D:GLY109 3.6 8.6 1.0
O D:TYR110 3.6 10.9 1.0
C D:GLY109 3.7 9.5 1.0
CB D:TYR110 3.8 10.8 1.0
CA D:TYR110 3.9 9.5 1.0
O D:THR108 4.0 10.6 1.0
O D:HOH329 4.0 24.6 1.0
C D:TYR110 4.2 9.2 1.0
O D:TYR82 4.3 16.5 1.0
O A:HOH438 4.3 19.5 1.0
CG D:TYR82 4.3 9.7 1.0
O A:HOH393 4.4 24.3 1.0
O D:ASN81 4.5 14.2 1.0
O D:HOH337 4.6 16.9 1.0
N D:GLY109 4.6 9.1 1.0
CA D:TYR82 4.7 11.3 1.0
C D:THR108 4.7 9.6 1.0
C D:TYR82 4.8 13.1 1.0
O D:GLY109 4.9 9.6 1.0
CD2 D:TYR82 4.9 11.1 1.0

Reference:

A.Gabdulkhakov, S.Tishchenko, A.Lisov, A.Leontievsky. Crystal Structure of L1 Protease of Lysobacter Sp. XL1 To Be Published.
Page generated: Sat Jul 12 05:37:09 2025

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