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Nickel in PDB 5n2a: Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form

Enzymatic activity of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form

All present enzymatic activity of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form:
2.8.4.1;

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form, PDB code: 5n2a was solved by T.Wagner, C.E.Wegner, U.Ermler, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.85 / 2.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 127.699, 127.699, 160.376, 90.00, 90.00, 120.00
R / Rfree (%) 19.8 / 22.1

Other elements in 5n2a:

The structure of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form also contains other interesting chemical elements:

Potassium (K) 1 atom
Bromine (Br) 1 atom

Nickel Binding Sites:

The binding sites of Nickel atom in the Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form (pdb code 5n2a). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form, PDB code: 5n2a:

Nickel binding site 1 out of 1 in 5n2a

Go back to Nickel Binding Sites List in 5n2a
Nickel binding site 1 out of 1 in the Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni603

b:59.4
occ:1.00
 NI A:F43603 0.0 59.4 1.0
ND A:F43603 2.0 59.2 1.0
NB A:F43603 2.0 61.0 1.0
NC A:F43603 2.0 60.3 1.0
NA A:F43603 2.1 59.6 1.0
C4B A:F43603 2.9 62.2 1.0
C1A A:F43603 3.0 59.2 1.0
C1C A:F43603 3.0 60.3 1.0
C1D A:F43603 3.0 59.4 1.0
C4D A:F43603 3.1 58.6 1.0
C4C A:F43603 3.1 60.2 1.0
C1B A:F43603 3.1 61.3 1.0
C4A A:F43603 3.2 59.2 1.0
S1 A:COM601 3.2 70.9 1.0
CHA A:F43603 3.2 58.8 1.0
CHB A:F43603 3.3 59.8 1.0
CHC A:F43603 3.3 61.2 1.0
CHD A:F43603 3.4 59.8 1.0
N5B A:F43603 3.7 62.0 1.0
C1 A:COM601 3.7 74.6 1.0
C3A A:F43603 4.2 58.4 1.0
C3B A:F43603 4.2 63.4 1.0
C2A A:F43603 4.3 58.4 1.0
C2D A:F43603 4.3 58.8 1.0
C3D A:F43603 4.3 58.1 1.0
C2C A:F43603 4.3 60.4 1.0
C3C A:F43603 4.4 60.5 1.0
C2B A:F43603 4.4 61.9 1.0
CAA A:F43603 4.6 57.9 1.0
OH A:TYR335 4.6 42.8 1.0
C2 A:COM601 4.6 77.8 1.0
OH B:TYR368 4.7 97.8 1.0
CAB A:F43603 4.8 65.9 1.0
C7D A:F43603 4.9 59.5 1.0
C6B A:F43603 4.9 62.0 1.0

Reference:

T.Wagner, C.E.Wegner, J.Kahnt, U.Ermler, S.Shima. Phylogenetic and Structural Comparisons of the Three Types of Methyl Coenzyme M Reductase From Methanococcales and Methanobacteriales. J.Bacteriol. V. 199 2017.
ISSN: ESSN 1098-5530
PubMed: 28559298
DOI: 10.1128/JB.00197-17
Page generated: Thu Oct 10 06:40:50 2024

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