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Chlorine in PDB 2fyf: Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis

Enzymatic activity of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis

All present enzymatic activity of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis:
2.6.1.52;

Protein crystallography data

The structure of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis, PDB code: 2fyf was solved by F.Coulibaly, E.Lassalle, E.N.Baker, Mycobacterium Tuberculosisstructural Proteomics Project (Xmtb), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.93 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.478, 94.056, 101.063, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 16.6

Other elements in 2fyf:

The structure of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis also contains other interesting chemical elements:

Platinum (Pt) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis (pdb code 2fyf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 9 binding sites of Chlorine where determined in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis, PDB code: 2fyf:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Chlorine binding site 1 out of 9 in 2fyf

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Chlorine binding site 1 out of 9 in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1378

b:16.3
occ:0.35
CL1 A:PC41378 0.0 16.3 0.3
PT A:PC41378 2.2 31.6 0.3
ND1 A:HIS8 2.8 25.5 1.0
CL2 A:PC41378 2.9 37.1 0.3
CE1 A:HIS8 3.3 25.7 1.0
N A:LEU9 3.4 17.7 1.0
O A:LEU9 3.5 13.9 1.0
CG A:HIS8 3.7 23.1 1.0
CA A:HIS8 3.7 20.6 1.0
CB A:ALA332 3.8 5.5 1.0
CG2 A:ILE329 3.8 6.8 1.0
CG1 A:ILE329 3.9 6.6 1.0
CA A:ILE329 3.9 5.9 1.0
ND2 A:ASN333 4.0 8.2 1.0
C A:HIS8 4.0 19.8 1.0
CB A:ILE329 4.1 5.3 1.0
CB A:HIS8 4.2 21.9 1.0
O A:ILE329 4.3 6.5 1.0
C A:LEU9 4.3 14.1 1.0
CA A:LEU9 4.3 15.9 1.0
NE2 A:HIS8 4.4 27.2 1.0
CL3 A:PC41378 4.5 40.9 0.3
CD2 A:HIS8 4.5 26.1 1.0
C A:ILE329 4.6 5.5 1.0
CB A:LEU9 4.6 15.8 1.0
N A:HIS8 4.8 21.9 1.0

Chlorine binding site 2 out of 9 in 2fyf

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Chlorine binding site 2 out of 9 in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1378

b:37.1
occ:0.35
CL2 A:PC41378 0.0 37.1 0.3
PT A:PC41378 1.9 31.6 0.3
CL1 A:PC41378 2.9 16.3 0.3
CL3 A:PC41378 2.9 40.9 0.3
ND1 A:HIS8 3.9 25.5 1.0
CB A:ALA332 4.1 5.5 1.0
CA A:HIS8 4.5 20.6 1.0
CB A:HIS8 4.7 21.9 1.0
CG A:HIS8 4.8 23.1 1.0
CE1 A:HIS8 4.8 25.7 1.0
CG1 A:ILE329 4.9 6.6 1.0
O A:LYS328 4.9 6.0 1.0

Chlorine binding site 3 out of 9 in 2fyf

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Chlorine binding site 3 out of 9 in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1378

b:40.9
occ:0.35
CL3 A:PC41378 0.0 40.9 0.3
PT A:PC41378 2.3 31.6 0.3
CL2 A:PC41378 2.9 37.1 0.3
ND1 A:HIS8 3.4 25.5 1.0
CB A:HIS8 3.7 21.9 1.0
CG A:HIS8 3.8 23.1 1.0
CE1 A:HIS8 4.4 25.7 1.0
CA A:HIS8 4.4 20.6 1.0
CL1 A:PC41378 4.5 16.3 0.3
N A:HIS8 4.9 21.9 1.0
CD2 A:HIS8 5.0 26.1 1.0

Chlorine binding site 4 out of 9 in 2fyf

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Chlorine binding site 4 out of 9 in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2378

b:16.6
occ:0.22
CL1 B:PC42378 0.0 16.6 0.2
PT B:PC42378 2.1 17.2 0.2
CL4 B:PC42378 2.8 22.4 0.2
CL2 B:PC42378 3.0 11.1 0.2
O B:HOH2775 3.2 46.6 1.0
CD1 B:TRP267 3.8 7.3 1.0
O B:HOH2523 3.8 24.5 1.0
CA B:TRP267 3.9 7.0 1.0
CB B:TRP267 4.0 7.5 1.0
OE1 B:GLU263 4.0 14.1 0.5
CL3 B:PC42378 4.3 12.0 0.2
CG B:TRP267 4.3 7.8 1.0
N B:TRP267 4.4 7.3 1.0
C B:ASP266 4.9 7.5 1.0
O B:HOH2702 4.9 35.2 1.0
CD B:GLU263 5.0 10.4 0.5
NE1 B:TRP267 5.0 7.6 1.0
O B:ASP266 5.0 8.2 1.0

Chlorine binding site 5 out of 9 in 2fyf

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Chlorine binding site 5 out of 9 in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2378

b:11.1
occ:0.22
CL2 B:PC42378 0.0 11.1 0.2
PT B:PC42378 2.2 17.2 0.2
CL1 B:PC42378 3.0 16.6 0.2
CL3 B:PC42378 3.2 12.0 0.2
NH1 B:ARG30 3.5 11.9 1.0
CG B:GLU32 3.8 12.8 1.0
CD1 B:TRP267 3.9 7.3 1.0
OE1 B:GLU263 4.2 14.1 0.5
OE2 B:GLU32 4.5 19.1 1.0
NE1 B:TRP267 4.5 7.6 1.0
CL4 B:PC42378 4.5 22.4 0.2
CZ B:ARG30 4.6 8.4 1.0
CD B:GLU32 4.7 14.4 1.0
CG B:TRP267 4.7 7.8 1.0
NH2 B:ARG30 4.7 11.2 1.0
CB B:GLU32 4.8 10.7 1.0

Chlorine binding site 6 out of 9 in 2fyf

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Chlorine binding site 6 out of 9 in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2378

b:12.0
occ:0.22
CL3 B:PC42378 0.0 12.0 0.2
PT B:PC42378 2.2 17.2 0.2
OE1 B:GLU263 2.5 14.1 0.5
CG B:GLU263 2.6 7.9 0.5
CD B:GLU263 3.0 10.4 0.5
NH2 B:ARG30 3.1 11.2 1.0
CL2 B:PC42378 3.2 11.1 0.2
NH1 B:ARG30 3.3 11.9 1.0
CL4 B:PC42378 3.5 22.4 0.2
CZ B:ARG30 3.6 8.4 1.0
CA B:GLN33 3.6 9.6 1.0
CB B:GLN33 3.7 11.1 1.0
CG B:GLN33 3.9 8.2 1.0
CB B:GLU263 4.0 7.9 0.5
CB B:GLU263 4.0 7.7 0.5
N B:GLN33 4.0 10.8 1.0
O B:GLU263 4.1 7.0 1.0
OE1 B:GLU263 4.2 11.6 0.5
OE2 B:GLU263 4.2 13.2 0.5
CL1 B:PC42378 4.3 16.6 0.2
O B:GLU32 4.4 11.0 1.0
C B:GLU32 4.4 10.8 1.0
C B:GLU263 4.5 7.2 1.0
CG B:GLU32 4.6 12.8 1.0
CB B:TRP267 4.7 7.5 1.0
CA B:GLU263 4.7 6.9 0.5
CA B:GLU263 4.7 7.0 0.5
CG B:GLU263 4.8 9.0 0.5
O B:HOH2702 4.8 35.2 1.0
NE B:ARG30 4.9 10.7 1.0
CG2 B:THR36 4.9 9.8 1.0
CD B:GLU263 5.0 9.5 0.5
C B:GLN33 5.0 9.3 1.0

Chlorine binding site 7 out of 9 in 2fyf

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Chlorine binding site 7 out of 9 in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2378

b:22.4
occ:0.22
CL4 B:PC42378 0.0 22.4 0.2
PT B:PC42378 2.3 17.2 0.2
OE1 B:GLU263 2.6 14.1 0.5
CL1 B:PC42378 2.8 16.6 0.2
O B:HOH2775 2.8 46.6 1.0
O B:GLU263 2.9 7.0 1.0
CD B:GLU263 2.9 10.4 0.5
O B:HOH2729 3.2 38.3 1.0
OE1 B:GLU263 3.2 11.6 0.5
OE2 B:GLU263 3.4 13.2 0.5
N B:TRP267 3.5 7.3 1.0
CB B:ASP266 3.5 8.0 1.0
CL3 B:PC42378 3.5 12.0 0.2
CG B:GLU263 3.6 7.9 0.5
C B:GLU263 3.8 7.2 1.0
CA B:TRP267 3.9 7.0 1.0
CB B:TRP267 3.9 7.5 1.0
C B:ASP266 4.0 7.5 1.0
CA B:GLU263 4.0 7.0 0.5
CA B:GLU263 4.0 6.9 0.5
O B:HOH2702 4.2 35.2 1.0
CA B:ASP266 4.3 7.3 1.0
CD B:GLU263 4.3 9.5 0.5
CB B:GLU263 4.3 7.9 0.5
CB B:GLU263 4.4 7.7 0.5
CL2 B:PC42378 4.5 11.1 0.2
O B:ASP266 4.7 8.2 1.0
CG B:ASP266 4.7 12.5 1.0
OD2 B:ASP266 4.7 15.5 1.0
N B:ASP266 4.8 7.1 1.0
CG B:GLU263 4.9 9.0 0.5

Chlorine binding site 8 out of 9 in 2fyf

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Chlorine binding site 8 out of 9 in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2383

b:16.2
occ:0.35
CL1 B:PC42383 0.0 16.2 0.3
PT B:PC42383 2.2 32.3 0.3
CL2 B:PC42383 2.9 37.9 0.3
ND1 B:HIS8 2.9 25.1 1.0
CE1 B:HIS8 3.4 26.7 1.0
N B:LEU9 3.5 18.9 1.0
O B:LEU9 3.7 15.6 1.0
CG1 B:ILE329 3.8 7.2 1.0
CG2 B:ILE329 3.9 7.2 1.0
CG B:HIS8 3.9 24.5 1.0
CB B:ALA332 3.9 6.9 1.0
CA B:ILE329 3.9 6.2 1.0
CA B:HIS8 3.9 21.8 1.0
CB B:ILE329 4.1 5.9 1.0
ND2 B:ASN333 4.2 8.7 1.0
C B:HIS8 4.2 21.2 1.0
CA B:LEU9 4.4 17.3 1.0
NE2 B:HIS8 4.4 27.4 1.0
O B:ILE329 4.4 5.4 1.0
C B:LEU9 4.4 15.8 1.0
CB B:HIS8 4.4 22.8 1.0
CB B:LEU9 4.6 17.0 1.0
CD2 B:HIS8 4.6 26.4 1.0
C B:ILE329 4.7 5.4 1.0
CD1 B:ILE329 5.0 8.1 1.0
N B:ILE329 5.0 6.3 1.0

Chlorine binding site 9 out of 9 in 2fyf

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Chlorine binding site 9 out of 9 in the Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Structure of A Putative Phosphoserine Aminotransferase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2383

b:37.9
occ:0.35
CL2 B:PC42383 0.0 37.9 0.3
PT B:PC42383 2.0 32.3 0.3
CL1 B:PC42383 2.9 16.2 0.3
ND1 B:HIS8 4.1 25.1 1.0
CB B:ALA332 4.2 6.9 1.0
CE1 B:HIS8 4.8 26.7 1.0
CA B:HIS8 4.9 21.8 1.0
CG1 B:ILE329 5.0 7.2 1.0

Reference:

F.Coulibaly, E.Lassalle, H.M.Baker, E.N.Baker. Structure of Phosphoserine Aminotransferase From Mycobacterium Tuberculosis. Acta Crystallogr.,Sect.D V. 68 553 2012.
ISSN: ISSN 0907-4449
PubMed: 22525753
DOI: 10.1107/S0907444912004829
Page generated: Wed Oct 28 10:36:24 2020

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