PDBsum entry 5a8w

Transferase

PDB id: 5a8w

Contents

Protein chains

548 a.a.

442 a.a.

263 a.a.

Ligands

COM

TP7 ×4

ACT ×11

F43-COM ×2

F43

COM-F43

Metals

_NA

Waters ×2915

PDB id:

5a8w

Name:

Transferase

Title:

Methyl-coenzyme m reductase ii from methanothermobacter wolfeii at 1. 8 a resolution

Structure:

Methyl-coenzyme m ii reductase. Chain: a, d, g, j. Other_details: in chain a, d, g and j, residue 261 is a n1- methylhistidine. Residue 275 is a c5-(s)-methylarginine. Residue 403 is a c2-(s)-methylglutamine. Residue 448 is a thioglycine. Residue 455 is a s-methylcysteine. Methyl-coenzyme m reductase ii. Chain: b, e, h, k. Methyl-coenzyme m reductase ii.

Source:

Methanothermobacter wolfeii. Organism_taxid: 145261. Atcc: dsm 2970. Other_details: german collection of microorganisms (dsm). Other_details: german collection of microorganisms (dsm)

Resolution:

1.80Å R-factor: 0.167 R-free: 0.201

Authors:

T.Wagner,U.Ermler

Key ref:

T.Wagner et al. (2016). Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation. Angew Chem Int Ed Engl, 55, 10630-10633. PubMed id: 27467699 DOI: 10.1002/anie.201603882

Date:

17-Jul-15 Release date: 03-Aug-16

Protein chains

H7CHY2  (H7CHY2_METWO) -  coenzyme-B sulfoethylthiotransferase (Fragment) from Methanothermobacter wolfeii

Seq: 381 a.a.

Struc: 548 a.a.*

Protein chains

A0A1C7D1E4  (A0A1C7D1E4_METWO) -  Methyl-coenzyme M reductase subunit beta from Methanothermobacter wolfeii

Seq: 443 a.a.

Struc: 442 a.a.

Protein chains

A0A1C7D1E5  (A0A1C7D1E5_METWO) -  Methyl-coenzyme M reductase subunit gamma from Methanothermobacter wolfeii

Seq: 265 a.a.

Struc: 263 a.a.

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F, G, H, I, J, K, L: E.C.2.8.4.1 - coenzyme-B sulfoethylthiotransferase.
• Pathway: Methane Biosynthesis
• Reaction: coenzyme B + methyl-coenzyme M = methane + coenzyme M-coenzyme B heterodisulfide

coenzyme B (Bound ligand (Het Group name = TP7) corresponds exactly) + methyl-coenzyme M (Bound ligand (Het Group name = COM) matches with 87.50% similarity) = methane + coenzyme M-coenzyme B heterodisulfide

• Cofactor: Coenzyme F430

Coenzyme F430 (Bound ligand (Het Group name = F43) matches with 96.83% similarity)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1002/anie.201603882

Angew Chem Int Ed Engl 55:10630-10633 (2016)

PubMed id: 27467699

Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation.

T.Wagner, J.Kahnt, U.Ermler, S.Shima.

ABSTRACT

No abstract given.