Zinc in PDB 8g3h: Structure of Cobalamin-Dependent Methionine Synthase (Meth) in A Resting State

Enzymatic activity of Structure of Cobalamin-Dependent Methionine Synthase (Meth) in A Resting State

All present enzymatic activity of Structure of Cobalamin-Dependent Methionine Synthase (Meth) in A Resting State:
2.1.1.13;

Other elements in 8g3h:

The structure of Structure of Cobalamin-Dependent Methionine Synthase (Meth) in A Resting State also contains other interesting chemical elements:

Cobalt (Co) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Cobalamin-Dependent Methionine Synthase (Meth) in A Resting State (pdb code 8g3h). 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 Cobalamin-Dependent Methionine Synthase (Meth) in A Resting State, PDB code: 8g3h:

Zinc binding site 1 out of 1 in 8g3h

Go back to Zinc Binding Sites List in 8g3h
Zinc binding site 1 out of 1 in the Structure of Cobalamin-Dependent Methionine Synthase (Meth) in A Resting State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Cobalamin-Dependent Methionine Synthase (Meth) in A Resting State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1201

b:21.2
occ:1.00
SG A:CYS256 2.3 12.4 1.0
SG A:CYS323 2.4 19.1 1.0
SG A:CYS322 3.2 16.4 1.0
OD1 A:ASN255 3.3 9.4 1.0
CB A:CYS256 3.9 12.4 1.0
OD1 A:ASN283 4.0 15.8 1.0
ND2 A:ASN283 4.0 15.8 1.0
CB A:CYS323 4.1 19.1 1.0
OG1 A:THR192 4.3 9.3 1.0
CA A:CYS256 4.3 12.4 1.0
N A:CYS256 4.3 12.4 1.0
CG A:ASN255 4.4 9.4 1.0
N A:CYS323 4.4 19.1 1.0
CG A:ASN283 4.4 15.8 1.0
CB A:CYS322 4.8 16.4 1.0
CA A:CYS323 4.8 19.1 1.0
ND2 A:ASN255 4.9 9.4 1.0
CG2 A:THR192 4.9 9.3 1.0

Reference:

M.B.Watkins, H.Wang, A.Burnim, N.Ando. Conformational Switching and Flexibility in Cobalamin-Dependent Methionine Synthase Studied By Small-Angle X-Ray Scattering and Cryoelectron Microscopy. Proc.Natl.Acad.Sci.Usa V. 120 31120 2023.
ISSN: ESSN 1091-6490
PubMed: 37339208
DOI: 10.1073/PNAS.2302531120
Page generated: Wed Oct 30 20:41:58 2024

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