Atomistry » Calcium » PDB 3slp-3t25 » 3sqg
Atomistry »
  Calcium »
    PDB 3slp-3t25 »
      3sqg »

Calcium in PDB 3sqg: Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats

Enzymatic activity of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats

All present enzymatic activity of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats:
2.8.4.1;

Protein crystallography data

The structure of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats, PDB code: 3sqg was solved by S.Shima, M.Krueger, T.Weinert, U.Demmer, R.K.Thauer, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.58 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 128.860, 412.490, 165.510, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 20.6

Other elements in 3sqg:

The structure of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats also contains other interesting chemical elements:

Nickel (Ni) 3 atoms
Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats (pdb code 3sqg). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats, PDB code: 3sqg:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 3sqg

Go back to Calcium Binding Sites List in 3sqg
Calcium binding site 1 out of 2 in the Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca587

b:24.7
occ:1.00
O A:THR232 2.6 21.2 1.0
O D:THR232 2.6 21.5 1.0
O D:ARG230 2.8 21.9 1.0
O A:ARG230 2.9 22.6 1.0
O A:ALA229 2.9 20.9 1.0
O D:ALA229 3.0 21.9 1.0
C D:ARG230 3.5 19.9 1.0
C A:ARG230 3.6 22.3 1.0
O D:HOH685 3.6 21.7 1.0
C A:THR232 3.6 22.6 1.0
O A:HOH681 3.6 18.8 1.0
C D:THR232 3.7 20.3 1.0
CA A:ARG230 3.8 23.1 1.0
CA D:ARG230 3.9 21.1 1.0
C A:ALA229 4.0 22.3 1.0
C D:ALA229 4.0 21.3 1.0
N A:THR232 4.2 21.5 1.0
O A:HOH662 4.2 19.1 1.0
N D:THR232 4.2 20.6 1.0
O D:HOH607 4.3 20.6 1.0
NZ D:LYS110 4.3 19.4 1.0
N A:ARG230 4.4 18.4 1.0
NZ A:LYS110 4.4 21.8 1.0
CA A:THR232 4.4 22.0 1.0
N D:ARG230 4.5 19.2 1.0
C A:GLN231 4.5 22.5 1.0
C D:GLN231 4.5 21.8 1.0
CA D:THR232 4.5 18.3 1.0
N A:ASP233 4.5 22.2 1.0
N D:GLN231 4.5 19.7 1.0
N A:GLN231 4.6 20.7 1.0
CA A:ASP233 4.6 23.6 1.0
N D:ASP233 4.6 19.9 1.0
CA D:ASP233 4.7 19.2 1.0
O D:GLN231 4.8 20.3 1.0
O A:GLN231 4.9 21.7 1.0
CA D:GLN231 5.0 20.8 1.0

Calcium binding site 2 out of 2 in 3sqg

Go back to Calcium Binding Sites List in 3sqg
Calcium binding site 2 out of 2 in the Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of A Methyl-Coenzyme M Reductase Purified From Black Sea Mats within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Ca583

b:22.8
occ:0.50
O G:THR232 2.5 27.9 1.0
O G:ARG230 2.7 20.8 1.0
O G:ALA229 3.2 23.5 1.0
O G:HOH638 3.3 27.4 1.0
C G:ARG230 3.4 21.5 1.0
C G:THR232 3.6 25.9 1.0
CA G:ARG230 3.9 22.3 1.0
N G:THR232 4.0 25.7 1.0
C G:GLN231 4.2 25.3 1.0
C G:ALA229 4.3 24.9 1.0
CA G:THR232 4.3 25.9 1.0
N G:GLN231 4.4 24.3 1.0
O G:GLN231 4.5 24.7 1.0
O G:HOH605 4.5 22.9 1.0
N G:ARG230 4.6 23.9 1.0
N G:ASP233 4.6 23.6 1.0
CA G:GLN231 4.7 24.8 1.0
CA G:ASP233 4.8 21.5 1.0
NZ G:LYS110 4.9 28.9 1.0

Reference:

S.Shima, M.Krueger, T.Weinert, U.Demmer, J.Kahnt, R.K.Thauer, U.Ermler. Structure of A Methyl-Coenzyme M Reductase From Black Sea Mats That Oxidize Methane Anaerobically. Nature V. 481 98 2011.
ISSN: ISSN 0028-0836
PubMed: 22121022
DOI: 10.1038/NATURE10663
Page generated: Sat Dec 12 04:30:32 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy