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Zinc in PDB 4qqu: Crystal Structure of the Cobalamin-Independent Methionine Synthase Enzyme in A Closed Conformation

Enzymatic activity of Crystal Structure of the Cobalamin-Independent Methionine Synthase Enzyme in A Closed Conformation

All present enzymatic activity of Crystal Structure of the Cobalamin-Independent Methionine Synthase Enzyme in A Closed Conformation:
2.1.1.14;

Protein crystallography data

The structure of Crystal Structure of the Cobalamin-Independent Methionine Synthase Enzyme in A Closed Conformation, PDB code: 4qqu was solved by D.K.Ubhi, J.D.Robertus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 71.71 / 2.98
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.978, 99.102, 103.902, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 27.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Cobalamin-Independent Methionine Synthase Enzyme in A Closed Conformation (pdb code 4qqu). 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 Crystal Structure of the Cobalamin-Independent Methionine Synthase Enzyme in A Closed Conformation, PDB code: 4qqu:

Zinc binding site 1 out of 1 in 4qqu

Go back to Zinc Binding Sites List in 4qqu
Zinc binding site 1 out of 1 in the Crystal Structure of the Cobalamin-Independent Methionine Synthase Enzyme in A Closed Conformation


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 the Cobalamin-Independent Methionine Synthase Enzyme in A Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn802

b:33.4
occ:1.00
 SD A:HCS801 1.9 33.2 1.0
SG A:CYS659 2.2 24.2 1.0
NE2 A:HIS657 2.2 30.0 1.0
SG A:CYS739 2.4 22.8 1.0
CD2 A:HIS657 3.0 30.1 1.0
CB A:CYS659 3.1 26.0 1.0
CG A:HCS801 3.3 31.4 1.0
CE1 A:HIS657 3.3 31.5 1.0
CB A:CYS739 3.4 24.7 1.0
CB A:HCS801 3.9 30.7 1.0
CG A:HIS657 4.2 30.4 1.0
ND1 A:HIS657 4.3 31.2 1.0
CA A:CYS739 4.3 25.3 1.0
CE2 A:TYR660 4.4 24.7 1.0
CA A:CYS659 4.5 26.2 1.0
O A:HOH906 4.6 17.6 1.0
N8 A:39S805 4.6 21.0 1.0
CD2 A:TYR660 4.7 24.1 1.0
N A:CYS659 4.8 27.1 1.0
CB A:PRO616 4.8 26.4 1.0
C18 A:39S805 4.9 20.5 1.0
O A:ASP738 4.9 26.3 1.0
CG A:PRO616 4.9 26.8 1.0
N A:GLY740 5.0 26.2 1.0
C A:PHE658 5.0 28.7 1.0

Reference:

D.K.Ubhi, J.D.Robertus. The Cobalamin-Independent Methionine Synthase Enzyme Captured in A Substrate Induced Closed Conformation. J.Mol.Biol. 2014.
ISSN: ESSN 1089-8638
PubMed: 25545590
DOI: 10.1016/J.JMB.2014.12.014
Page generated: Sun Oct 27 06:44:28 2024

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