Brand  (β version)

PDB ID: 1HBM

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Ligands
Code Name Style Show Link
CL Chloride ion PoSSuM
F43 Factor 430 PoSSuM
GOL Glycerol PoSSuM
MG Magnesium ion PoSSuM
NA Sodium ion PoSSuM
SHT O-phosphono-N-{(2e)-7-[(2-sulfoethyl)dithio]hept-2-enoyl}-L-threonine 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 : 1HBM   PDBj   RCSB PDB   PDBe
Header : METHANOGENESIS
Title : METHYL-COENZYME M REDUCTASE ENZYME PRODUCT COMPLEX
Release Data : 2001-08-16
Compound :
mol_id molecule chains
1 METHYL-COENZYME M REDUCTASE I ALPHA SUBUNIT A,D
mol_id molecule chains
2 METHYL-COENZYME M REDUCTASE I BETA SUBUNIT B,E
mol_id molecule chains
3 METHYL-COENZYME M REDUCTASE I GAMMA SUBUNIT C,F
other_details: MCR-OX-SILENT STATE, ENZYME-SUBSTRATE COMPLEX
Source :
mol_id organism_scientific
1 METHANOTHERMOBACTER THERMAUTOTROPHICUS  (taxid:145262)
strain: MARBURG
cellular_location: CYTOPLASM
mol_id organism_scientific
2 METHANOTHERMOBACTER THERMAUTOTROPHICUS  (taxid:145262)
strain: MARBURG
cellular_location: CYTOPLASM
mol_id organism_scientific
3 METHANOTHERMOBACTER THERMAUTOTROPHICUS  (taxid:145262)
strain: MARBURG
cellular_location: CYTOPLASM
Authors : Ermler, U., Grabarse, W.
Keywords : METHANOGENESIS, BIOLOGICAL METHANOGENESIS, NI-ENZYME, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.8 Å )
Citation :

On the Mechanism of Biological Methane Formation: Structural Evidence for Conformational Changes in Methyl-Coenzyme M Reductase Upon Substrate Binding

Grabarse, W.,Mahlert, F.,Duin, E.C.  et al.
(2001)  J.Mol.Biol.  309 : 315

PubMed: 11491299
DOI: 10.1006/JMBI.2001.4647

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).