Brand  (β version)

PDB ID: 1MRO

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Ligands
Code Name Style Show Link
COM 1-thioethanesulfonic acid PoSSuM
F43 Factor 430 PoSSuM
GOL Glycerol PoSSuM
NA Sodium ion PoSSuM
TP7 Coenzyme B PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
Code Name Show
AGM 5-methyl-arginine
GL3 Thioglycin
MGN 2-methyl-glutamine
MHS N1-methylated histidine
SMC S-methylcysteine
Glycosylation
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Modification
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Structure summary

Code : 1MRO   PDBj   RCSB PDB   PDBe
Header : METHANOGENESIS
Title : METHYL-COENZYME M REDUCTASE
Release Data : 1998-11-11
Compound :
mol_id molecule chains
1 METHYL-COENZYME M REDUCTASE A,D
ec: 1.8.-.-
other_details: MCR-OX-SILENT STATE, ENZYME-SUBSTRATE COMPLEX
mol_id molecule chains
2 METHYL-COENZYME M REDUCTASE B,E
ec: 1.8.-.-
other_details: MCR-OX-SILENT STATE, ENZYME-SUBSTRATE COMPLEX
mol_id molecule chains
3 METHYL-COENZYME M REDUCTASE C,F
ec: 1.8.-.-
other_details: MCR-OX-SILENT STATE, ENZYME-SUBSTRATE COMPLEX
Source :
mol_id organism_scientific
1 Methanothermobacter marburgensis str. Marburg  (taxid:79929)
strain: MARBURG
cellular_location: CYTOPLASM
mol_id organism_scientific
2 Methanothermobacter marburgensis str. Marburg  (taxid:79929)
strain: MARBURG
cellular_location: CYTOPLASM
mol_id organism_scientific
3 Methanothermobacter marburgensis str. Marburg  (taxid:79929)
strain: MARBURG
cellular_location: CYTOPLASM
Authors : Ermler, U., Grabarse, W.
Keywords : BIOLOGICAL METHANOGENESIS, NI-ENZYME, OXIDOREDUCTASE, METHANOGENESIS
Exp. method : X-RAY DIFFRACTION ( 1.16 Å )
Citation :

Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.

Ermler, U.,Grabarse, W.,Shima, S.  et al.
(1997)  Science  278 : 1457 - 1462

PubMed: 9367957
DOI: 10.1126/science.278.5342.1457

Reaction

Chain : A, D
UniProt : P11558 (MCRA_METTM)
Reaction: EC: Evidence:
Physiological Direction:
coenzyme B + methyl-coenzyme M = methane + coenzyme M-coenzyme B heterodisulfide 2.8.4.1 PubMed:2269306, PubMed:25691570, PubMed:27140643, PubMed:3350018
left-to-right PubMed:27140643, PubMed:3350018
Cofactor: Evidence: Note:
coenzyme F430 ECO:0000269 | PubMed:3350018
ECO:0000269 | PubMed:9030728
ECO:0000269 | PubMed:9367957
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state (PubMed:9030728).
Chain : B, E
UniProt : P11560 (MCRB_METTM)
Reaction: EC: Evidence:
Physiological Direction:
coenzyme B + methyl-coenzyme M = methane + coenzyme M-coenzyme B heterodisulfide 2.8.4.1 PubMed:2269306, PubMed:25691570, PubMed:27140643, PubMed:3350018
left-to-right PubMed:27140643, PubMed:3350018
Cofactor: Evidence: Note:
coenzyme F430 ECO:0000269 | PubMed:3350018
ECO:0000269 | PubMed:9030728
ECO:0000269 | PubMed:9367957
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state (PubMed:9030728).
Chain : C, F
UniProt : P11562 (MCRG_METTM)
Reaction: EC: Evidence:
Physiological Direction:
coenzyme B + methyl-coenzyme M = methane + coenzyme M-coenzyme B heterodisulfide 2.8.4.1 PubMed:2269306, PubMed:25691570, PubMed:27140643, PubMed:3350018
left-to-right PubMed:27140643, PubMed:3350018
Cofactor: Evidence: Note:
coenzyme F430 ECO:0000269 | PubMed:3350018
ECO:0000269 | PubMed:9030728
ECO:0000269 | PubMed:9367957
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state (PubMed:9030728).