Atomistry » Zinc » PDB 1h71-1hld » 1hbu
Atomistry »
  Zinc »
    PDB 1h71-1hld »
      1hbu »

Zinc in PDB 1hbu: Methyl-Coenzyme M Reductase in the Mcr-RED1-Silent State in Complex with Coenzyme M

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase in the Mcr-RED1-Silent State in Complex with Coenzyme M, PDB code: 1hbu 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) 10.00 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 81.100, 116.500, 121.800, 90.00, 91.80, 90.00
R / Rfree (%) 16.2 / 21.1

Other elements in 1hbu:

The structure of Methyl-Coenzyme M Reductase in the Mcr-RED1-Silent State in Complex with Coenzyme M also contains other interesting chemical elements:

Nickel (Ni) 2 atoms
Magnesium (Mg) 13 atoms
Chlorine (Cl) 2 atoms
Sodium (Na) 9 atoms

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 1hbu

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


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 in the Mcr-RED1-Silent State in Complex with Coenzyme M within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1557

b:17.0
occ:0.50
O D:CYS218 2.8 11.8 1.0
O A:CYS218 2.8 14.3 1.0
O A:ARG216 2.8 12.8 1.0
O D:ARG216 2.8 14.1 1.0
O A:SER215 3.3 12.1 1.0
NH2 A:ARG102 3.4 11.8 1.0
O D:SER215 3.4 12.8 1.0
NH2 D:ARG102 3.5 7.5 1.0
C A:ARG216 3.6 12.7 1.0
C D:ARG216 3.6 13.9 1.0
O A:HOH2269 3.8 11.6 1.0
O D:HOH2274 3.8 9.9 1.0
C A:CYS218 3.8 14.2 1.0
CA A:ARG216 3.8 12.7 1.0
CA D:ARG216 3.9 13.2 1.0
C D:CYS218 3.9 10.9 1.0
CZ A:ARG102 3.9 13.3 1.0
NH1 D:ARG102 4.0 10.4 1.0
CZ D:ARG102 4.0 9.9 1.0
NH1 A:ARG102 4.0 12.8 1.0
N A:CYS218 4.3 11.1 1.0
C D:SER215 4.4 12.9 1.0
C A:SER215 4.4 13.7 1.0
N D:CYS218 4.4 10.0 1.0
C A:THR217 4.5 10.9 1.0
C D:THR217 4.5 11.0 1.0
CA A:ASP219 4.6 13.1 1.0
N D:ARG216 4.6 12.0 1.0
N A:ARG216 4.6 14.1 1.0
CA D:ASP219 4.6 11.5 1.0
N A:ASP219 4.6 14.8 1.0
N D:ASP219 4.7 10.5 1.0
N D:THR217 4.7 11.5 1.0
N A:THR217 4.7 10.8 1.0
CA A:CYS218 4.7 11.0 1.0
CA D:CYS218 4.7 11.2 1.0
O D:THR217 4.8 12.6 1.0
O A:THR217 4.8 10.6 1.0
NE A:ARG102 4.9 12.6 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: Sun Oct 13 02:05:55 2024

Last articles

Zn in 9FD2
Zn in 9GUW
Zn in 9GUX
Zn in 9F7C
Zn in 9GUR
Zn in 9F7A
Zn in 9DDE
Zn in 9DBY
Zn in 9EBZ
Zn in 9DGG
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy