Structure of PDB 1mro Chain E

Receptor sequence
>1mroE (length=442) Species: 79929 (Methanothermobacter marburgensis str. Marburg) [Search protein sequence]
AKFEDKVDLYDDRGNLVEEQVPLEALSPLRNPAIKSIVQGIKRTVAVNLE
GIENALKTAKVGGPACKIMGRELDLDIVGNAESIAAAAKEMIQVTEDDDT
NVELLGGGKRALVQVPSARFDVAAEYSAAPLVTATAFVQAIINEFDVSMY
DANMVKAAVLGRYPQSVEYMGANIATMLDIPQKLEGPGYALRNIMVNHVV
AATLKNTLQAAALSTILEQTAMFEMGDAVGAFERMHLLGLAYQGMNADNL
VFDLVKANGKEGTVGSVIADLVERALEDGVIKVEKELTDYKVYGTDDLAM
WNAYAAAGLMAATMVNQGAARAAQGVSSTLLYYNDLIEFETGLPSVDFGK
VEGTAVGFSFFSHSIYGGGGPGIFNGNHIVTRHSKGFAIPCVAAAMALDA
GTQMFSPEATSGLIKEVFSQVDEFREPLKYVVEAAAEIKNEI
3D structure
PDB1mro Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.
ChainE
Resolution1.16 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y367
Catalytic site (residue number reindexed from 1) Y366
Enzyme Commision number 2.8.4.1: coenzyme-B sulfoethylthiotransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 F43 E S365 I366 Y367 S364 I365 Y366
BS02 TP7 E F361 Y367 G369 H379 F360 Y366 G368 H378
BS03 COM E F361 Y367 F360 Y366
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0050524 coenzyme-B sulfoethylthiotransferase activity
Biological Process
GO:0015948 methanogenesis
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1mro, PDBe:1mro, PDBj:1mro
PDBsum1mro
PubMed9367957
UniProtP11560|MCRB_METTM Methyl-coenzyme M reductase I subunit beta (Gene Name=mcrB)

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