Structure of PDB 3m2u Chain E

Receptor sequence
>3m2uE (length=442) Species: 79929 (Methanothermobacter marburgensis str. Marburg) [Search protein sequence]
AKFEDKVDLYDDRGNLVEEQVPLEALSPLRNPAIKSIVQGIKRTVAVNLE
GIENALKTAKVGGPACKIMGRELDLDIVGNAESIAAAAKEMIQVTEDDDT
NVELLGGGKRALVQVPSARFDVAAEYSAAPLVTATAFVQAIINEFDVSMY
DANMVKAAVLGRYPQSVEYMGANIATMLDIPQKLEGPGYALRNIMVNHVV
AATLKNTLQAAALSTILEQTAMFEMGDAVGAFERMHLLGLAYQGMNADNL
VFDLVKANGKEGTVGSVIADLVERALEDGVIKVEKELTDYKVYGTDDLAM
WNAYAAAGLMAATMVNQGAARAAQGVSSTLLYYNDLIEFETGLPSVDFGK
VEGTAVGFSFFSHSIYGGGGPGIFNGNHIVTRHSKGFAIPCVAAAMALDA
GTQMFSPEATSGLIKEVFSQVDEFREPLKYVVEAAAEIKNEI
3D structure
PDB3m2u Structural insight into methyl-coenzyme M reductase chemistry using coenzyme B analogues.
ChainE
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 F362 Y367 G369 H379 F360 F361 Y366 G368 H378
BS03 COM E F361 Y367 F360 Y366
BS04 TXZ 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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3m2u, PDBe:3m2u, PDBj:3m2u
PDBsum3m2u
PubMed20707311
UniProtP11560|MCRB_METTM Methyl-coenzyme M reductase I subunit beta (Gene Name=mcrB)

[Back to BioLiP]