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Zinc in PDB 4cog: Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia

Enzymatic activity of Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia

All present enzymatic activity of Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia:
3.5.1.9;

Protein crystallography data

The structure of Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia, PDB code: 4cog was solved by L.Diaz-Saez, V.Srikannathasan, M.Zoltner, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 134.84 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 76.859, 50.120, 135.197, 90.00, 94.15, 90.00
R / Rfree (%) 14.886 / 18.431

Other elements in 4cog:

The structure of Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia also contains other interesting chemical elements:

Cadmium (Cd) 4 atoms
Magnesium (Mg) 8 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia (pdb code 4cog). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia, PDB code: 4cog:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4cog

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Zinc binding site 1 out of 4 in the Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:11.7
occ:1.00
 O2 A:GOL1213 1.9 14.6 1.0
OE2 A:GLU172 2.0 12.9 1.0
OD2 A:ASP54 2.1 11.1 1.0
NE2 A:HIS160 2.1 12.7 1.0
OE1 A:GLU172 2.6 13.2 1.0
CD A:GLU172 2.7 11.4 1.0
C2 A:GOL1213 2.9 17.8 1.0
CE1 A:HIS160 3.0 15.3 1.0
CG A:ASP54 3.0 10.3 1.0
CD2 A:HIS160 3.2 13.9 1.0
CD A:CD402 3.3 13.1 1.0
OD1 A:ASP54 3.4 11.3 1.0
C1 A:GOL1213 3.5 18.6 1.0
O1 A:GOL1213 4.1 18.0 1.0
CD2 A:HIS58 4.1 14.9 1.0
CG A:GLU172 4.2 11.2 1.0
C3 A:GOL1213 4.2 20.8 1.0
ND1 A:HIS160 4.2 12.6 1.0
CG A:HIS160 4.3 12.9 1.0
NE2 A:HIS58 4.3 14.9 1.0
CB A:ASP54 4.3 9.6 1.0
OG A:SER148 4.4 15.0 1.0
O3 A:GOL1213 4.4 17.5 1.0
CG2 A:ILE170 4.4 14.1 1.0
CD1 A:ILE170 4.4 13.0 1.0
O A:HOH2122 4.6 11.9 1.0
O A:PRO147 4.6 13.4 1.0
CA A:SER148 4.6 12.7 1.0
N A:LEU149 4.6 12.0 1.0
CB A:SER148 4.9 12.4 1.0

Zinc binding site 2 out of 4 in 4cog

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Zinc binding site 2 out of 4 in the Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:9.0
occ:1.00
 O2 B:GOL1213 2.0 13.1 1.0
OD2 B:ASP54 2.1 9.3 1.0
NE2 B:HIS160 2.1 12.1 1.0
OE2 B:GLU172 2.1 10.0 1.0
OE1 B:GLU172 2.6 11.8 1.0
CD B:GLU172 2.6 8.8 1.0
C2 B:GOL1213 2.8 12.9 1.0
CE1 B:HIS160 3.0 11.4 1.0
CG B:ASP54 3.0 8.6 1.0
CD2 B:HIS160 3.2 11.5 1.0
CD B:CD402 3.3 10.7 1.0
OD1 B:ASP54 3.4 9.1 1.0
C1 B:GOL1213 3.5 17.0 1.0
O1 B:GOL1213 4.0 11.7 1.0
CD2 B:HIS58 4.1 13.7 1.0
C3 B:GOL1213 4.1 19.0 1.0
ND1 B:HIS160 4.2 11.6 1.0
CG B:GLU172 4.2 9.1 1.0
NE2 B:HIS58 4.3 12.8 1.0
CG B:HIS160 4.3 11.8 1.0
OG B:SER148 4.3 11.5 1.0
CB B:ASP54 4.4 8.2 1.0
O3 B:GOL1213 4.4 14.1 1.0
CG2 B:ILE170 4.4 13.0 1.0
CD1 B:ILE170 4.5 12.2 1.0
O B:PRO147 4.6 11.1 1.0
CA B:SER148 4.6 10.7 1.0
O B:HOH2095 4.6 10.4 1.0
N B:LEU149 4.7 10.4 1.0
CB B:SER148 4.9 10.4 1.0

Zinc binding site 3 out of 4 in 4cog

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Zinc binding site 3 out of 4 in the Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn401

b:9.7
occ:1.00
 O2 C:GOL1213 2.0 10.5 1.0
OD2 C:ASP54 2.0 10.1 1.0
OE2 C:GLU172 2.0 11.3 1.0
NE2 C:HIS160 2.1 10.9 1.0
OE1 C:GLU172 2.6 11.3 1.0
CD C:GLU172 2.7 9.7 1.0
C2 C:GOL1213 2.8 13.2 1.0
CE1 C:HIS160 3.0 12.9 1.0
CG C:ASP54 3.0 10.2 1.0
CD2 C:HIS160 3.2 11.3 1.0
CD C:CD402 3.3 11.3 1.0
OD1 C:ASP54 3.4 9.8 1.0
C1 C:GOL1213 3.5 16.2 1.0
CD2 C:HIS58 4.1 13.6 1.0
O1 C:GOL1213 4.2 13.9 1.0
ND1 C:HIS160 4.2 11.8 1.0
C3 C:GOL1213 4.2 17.2 1.0
CG C:GLU172 4.2 9.9 1.0
CG C:HIS160 4.3 11.7 1.0
NE2 C:HIS58 4.3 13.6 1.0
CB C:ASP54 4.4 8.3 1.0
OG C:SER148 4.4 13.9 1.0
CD1 C:ILE170 4.4 11.3 1.0
CG2 C:ILE170 4.4 10.8 1.0
O3 C:GOL1213 4.5 14.1 1.0
O C:PRO147 4.6 11.7 1.0
O C:HOH2104 4.6 10.3 1.0
N C:LEU149 4.6 10.4 1.0
CA C:SER148 4.6 10.3 1.0
CB C:SER148 4.9 10.4 1.0

Zinc binding site 4 out of 4 in 4cog

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Zinc binding site 4 out of 4 in the Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Kynurenine Formamidase From Burkholderia Cenocepacia within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn401

b:9.8
occ:1.00
 OD2 D:ASP54 2.0 10.2 1.0
O2 D:GOL1214 2.0 11.8 1.0
OE2 D:GLU172 2.1 10.4 1.0
NE2 D:HIS160 2.1 11.7 1.0
OE1 D:GLU172 2.6 11.0 1.0
CD D:GLU172 2.7 9.5 1.0
C2 D:GOL1214 2.9 13.3 1.0
CG D:ASP54 3.0 9.1 1.0
CE1 D:HIS160 3.0 11.1 1.0
CD2 D:HIS160 3.1 10.1 1.0
CD D:CD402 3.3 10.7 1.0
OD1 D:ASP54 3.4 9.0 1.0
C1 D:GOL1214 3.6 15.6 1.0
CD2 D:HIS58 4.0 11.0 1.0
O1 D:GOL1214 4.1 14.1 1.0
CG D:GLU172 4.1 8.4 1.0
NE2 D:HIS58 4.2 11.6 1.0
ND1 D:HIS160 4.2 11.8 1.0
C3 D:GOL1214 4.2 18.2 1.0
CG D:HIS160 4.2 11.4 1.0
CB D:ASP54 4.3 8.7 1.0
OG D:SER148 4.3 12.1 1.0
CG2 D:ILE170 4.4 11.8 1.0
CD1 D:ILE170 4.4 11.8 1.0
O3 D:GOL1214 4.5 14.2 1.0
O D:HOH2073 4.6 11.0 1.0
CA D:SER148 4.6 10.4 1.0
N D:LEU149 4.6 10.7 1.0
O D:PRO147 4.7 11.6 1.0
CB D:SER148 4.9 10.9 1.0

Reference:

L.Diaz-Saez, V.Srikannathasan, M.Zoltner, W.N.Hunter. Structure of Bacterial Kynurenine Formamidase Reveals A Crowded Binuclear-Zinc Catalytic Site Primed to Generate A Potent Nucleophile. Biochem.J. V. 462 581 2014.
ISSN: ISSN 0264-6021
PubMed: 24942958
DOI: 10.1042/BJ20140511
Page generated: Sat Oct 26 20:54:13 2024

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