Structure of PDB 5a0y Chain E

Receptor sequence
>5a0yE (length=442) Species: 145263 (Methanothermobacter marburgensis) [Search protein sequence]
AKFEDKVDLYDDRGNLVEEQVPLEALSPLRNPAIKSIVQGIKRTVAVNLE
GIENALKTAKVGGPACKIMGRELDLDIVGNAESIAAAAKEMIQVTEDDDT
NVELLGGGKRALVQVPSARFDVAAEYSAAPLVTATAFVQAIINEFDVSMY
DANMVKAAVLGRYPQSVEYMGANIATMLDIPQKLEGPGYALRNIMVNHVV
AATLKNTLQAAALSTILEQTAMFEMGDAVGAFERMHLLGLAYQGMNADNL
VFDLVKANGKEGTVGSVIADLVERALEDGVIKVEKELTDYKVYGTDDLAM
WNAYAAAGLMAATMVNQGAARAAQGVSSTLLYYNDLIEFETGLPSVDFGK
VEGTAVGFSFFSHSIYGGGGPGIFNGNHIVTRHSKGFAIPCVAAAMALDA
GTQMFSPEATSGLIKEVFSQVDEFREPLKYVVEAAAEIKNEI
3D structure
PDB5a0y Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation.
ChainE
Resolution1.1 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 COM E F361 Y367 F360 Y366
BS03 TP7 E F361 F362 Y367 G369 H379 F360 F361 Y366 G368 H378
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:5a0y, PDBe:5a0y, PDBj:5a0y
PDBsum5a0y
PubMed27467699
UniProtP11560|MCRB_METTM Methyl-coenzyme M reductase I subunit beta (Gene Name=mcrB)

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