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Zinc in PDB 4p3x: Structure of the FE4S4 Quinolinate Synthase Nada From Thermotoga Maritima

Enzymatic activity of Structure of the FE4S4 Quinolinate Synthase Nada From Thermotoga Maritima

All present enzymatic activity of Structure of the FE4S4 Quinolinate Synthase Nada From Thermotoga Maritima:
2.5.1.72;

Protein crystallography data

The structure of Structure of the FE4S4 Quinolinate Synthase Nada From Thermotoga Maritima, PDB code: 4p3x was solved by M.V.Cherrier, A.Chan, C.Darnault, D.Reichmann, P.Amara, S.Ollagnier Dechoudens, J.C.Fontecilla-Camps, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.14 / 1.65
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 42.920, 157.210, 93.940, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23.9

Other elements in 4p3x:

The structure of Structure of the FE4S4 Quinolinate Synthase Nada From Thermotoga Maritima also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the FE4S4 Quinolinate Synthase Nada From Thermotoga Maritima (pdb code 4p3x). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of the FE4S4 Quinolinate Synthase Nada From Thermotoga Maritima, PDB code: 4p3x:

Zinc binding site 1 out of 1 in 4p3x

Go back to Zinc Binding Sites List in 4p3x
Zinc binding site 1 out of 1 in the Structure of the FE4S4 Quinolinate Synthase Nada From Thermotoga Maritima


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the FE4S4 Quinolinate Synthase Nada From Thermotoga Maritima within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:20.0
occ:1.00
 O A:MET-6 2.1 19.2 1.0
NE2 A:HIS-1 2.1 17.8 1.0
N A:MET-6 2.2 22.1 1.0
C A:MET-6 2.9 20.5 1.0
CA A:MET-6 3.1 21.8 1.0
CE1 A:HIS-1 3.1 17.7 1.0
CD2 A:HIS-1 3.1 17.1 1.0
CB A:MET-6 4.2 23.8 1.0
N A:HIS-5 4.2 20.6 1.0
ND1 A:HIS-1 4.2 16.8 1.0
CG A:HIS-1 4.3 15.7 1.0
CG A:MET-6 4.3 26.0 1.0
O A:HOH444 4.5 26.6 1.0
C A:HIS-5 4.8 19.9 1.0
CA A:HIS-5 4.9 20.6 1.0

Reference:

M.V.Cherrier, A.Chan, C.Darnault, D.Reichmann, P.Amara, S.Ollagnier De Choudens, J.C.Fontecilla-Camps. The Crystal Structure of FE4S4 Quinolinate Synthase Unravels An Enzymatic Dehydration Mechanism That Uses Tyrosine and A Hydrolase-Type Triad. J.Am.Chem.Soc. V. 136 5253 2014.
ISSN: ESSN 1520-5126
PubMed: 24650327
DOI: 10.1021/JA501431B
Page generated: Sun Oct 27 04:13:27 2024

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