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Zinc in PDB 1mro: Methyl-Coenzyme M Reductase

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase, PDB code: 1mro was solved by U.Ermler, W.Grabarse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.16
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 81.720, 116.883, 122.582, 90.00, 92.02, 90.00
R / Rfree (%) 19.7 / 20.7

Other elements in 1mro:

The structure of Methyl-Coenzyme M Reductase also contains other interesting chemical elements:

Nickel (Ni) 2 atoms
Sodium (Na) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Methyl-Coenzyme M Reductase (pdb code 1mro). 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 Methyl-Coenzyme M Reductase, PDB code: 1mro:

Zinc binding site 1 out of 1 in 1mro

Go back to Zinc Binding Sites List in 1mro
Zinc binding site 1 out of 1 in the Methyl-Coenzyme M Reductase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Methyl-Coenzyme M Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn801

b:11.6
occ:1.00
O A:CYS218 2.7 11.8 1.0
O D:CYS218 2.7 11.3 1.0
O D:ARG216 2.8 11.2 1.0
O A:ARG216 2.8 11.3 1.0
O A:SER215 3.3 11.6 1.0
O D:SER215 3.4 11.3 1.0
NH1 A:ARG102 3.4 10.8 1.0
NH1 D:ARG102 3.5 13.2 1.0
C A:ARG216 3.5 11.3 1.0
C D:ARG216 3.6 11.3 1.0
C A:CYS218 3.8 11.8 1.0
C D:CYS218 3.8 11.4 1.0
CA A:ARG216 3.8 11.3 1.0
CA D:ARG216 3.8 11.3 1.0
O A:HOH7528 3.9 18.5 1.0
O D:HOH7542 3.9 16.6 1.0
CZ A:ARG102 4.1 10.6 1.0
CZ D:ARG102 4.1 13.3 1.0
NH2 A:ARG102 4.1 10.8 1.0
NH2 D:ARG102 4.1 13.2 1.0
C A:SER215 4.3 11.5 1.0
C D:SER215 4.4 11.2 1.0
N A:CYS218 4.4 11.5 1.0
N D:CYS218 4.4 11.2 1.0
CA A:ASP219 4.6 11.9 1.0
N A:ARG216 4.6 11.4 1.0
CA D:ASP219 4.6 11.6 1.0
N A:ASP219 4.6 11.8 1.0
N D:ARG216 4.6 11.2 1.0
C A:THR217 4.6 11.4 1.0
N A:THR217 4.6 11.3 1.0
N D:ASP219 4.6 11.3 1.0
C D:THR217 4.6 11.3 1.0
N D:THR217 4.6 11.2 1.0
CA A:CYS218 4.7 11.7 1.0
CA D:CYS218 4.7 11.3 1.0
O A:THR217 4.9 11.5 1.0
O D:THR217 4.9 11.4 1.0

Reference:

U.Ermler, W.Grabarse, S.Shima, M.Goubeaud, R.K.Thauer. Crystal Structure of Methyl-Coenzyme M Reductase: the Key Enzyme of Biological Methane Formation. Science V. 278 1457 1997.
ISSN: ISSN 0036-8075
PubMed: 9367957
DOI: 10.1126/SCIENCE.278.5342.1457
Page generated: Wed Dec 16 02:57:21 2020

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