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Zinc in PDB 1hbo: Methyl-Coenzyme M Reductase Mcr-RED1-Silent

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase Mcr-RED1-Silent, PDB code: 1hbo was solved by W.Grabarse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.78
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 81.700, 117.300, 122.400, 90.00, 92.00, 90.00
R / Rfree (%) 17.7 / 21.3

Other elements in 1hbo:

The structure of Methyl-Coenzyme M Reductase Mcr-RED1-Silent also contains other interesting chemical elements:

Nickel (Ni) 2 atoms
Magnesium (Mg) 4 atoms
Chlorine (Cl) 2 atoms
Sodium (Na) 8 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Methyl-Coenzyme M Reductase Mcr-RED1-Silent (pdb code 1hbo). 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 Mcr-RED1-Silent, PDB code: 1hbo:

Zinc binding site 1 out of 1 in 1hbo

Go back to Zinc Binding Sites List in 1hbo
Zinc binding site 1 out of 1 in the Methyl-Coenzyme M Reductase Mcr-RED1-Silent


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 Mcr-RED1-Silent within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1556

b:23.4
occ:0.50
O A:CYS218 2.8 14.1 1.0
O D:CYS218 2.8 13.3 1.0
O A:ARG216 2.8 12.4 1.0
O D:ARG216 2.8 15.7 1.0
O A:SER215 3.4 11.8 1.0
O D:SER215 3.4 12.8 1.0
NH2 D:ARG102 3.5 9.4 1.0
NH2 A:ARG102 3.5 11.4 1.0
C A:ARG216 3.6 12.3 1.0
C D:ARG216 3.6 14.3 1.0
O A:HOH2265 3.8 13.4 1.0
CA D:ARG216 3.9 12.2 1.0
C A:CYS218 3.9 13.7 1.0
CA A:ARG216 3.9 11.6 1.0
O D:HOH2267 3.9 12.7 1.0
C D:CYS218 3.9 11.9 1.0
CZ A:ARG102 4.0 12.4 1.0
NH1 A:ARG102 4.0 13.3 1.0
CZ D:ARG102 4.0 10.8 1.0
NH1 D:ARG102 4.0 11.5 1.0
C D:SER215 4.4 11.9 1.0
C A:SER215 4.4 12.6 1.0
N A:CYS218 4.4 11.3 1.0
N D:CYS218 4.4 11.4 1.0
C D:THR217 4.5 11.2 1.0
C A:THR217 4.6 11.8 1.0
N D:ARG216 4.6 12.9 1.0
N A:THR217 4.6 11.5 1.0
N A:ASP219 4.7 12.9 1.0
CA D:ASP219 4.7 12.3 1.0
N A:ARG216 4.7 11.7 1.0
CA A:ASP219 4.7 13.3 1.0
N D:THR217 4.7 11.9 1.0
N D:ASP219 4.7 11.9 1.0
O D:THR217 4.7 11.9 1.0
CA D:CYS218 4.8 11.9 1.0
CA A:CYS218 4.8 11.3 1.0
O A:THR217 4.8 10.8 1.0
NE A:ARG102 5.0 11.8 1.0

Reference:

W.Grabarse, F.Mahlert, E.C.Duin, M.Goubeaud, S.Shima, R.K.Thauer, V.Lamzin, U.Ermler. On the Mechanism of Biological Methane Formation: Structural Evidence For Conformational Changes in Methyl-Coenzyme M Reductase Upon Substrate Binding J.Mol.Biol. V. 309 315 2001.
ISSN: ISSN 0022-2836
PubMed: 11491299
DOI: 10.1006/JMBI.2001.4647
Page generated: Wed Dec 16 02:51:06 2020

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