Structure of PDB 1hbm Chain A

Receptor sequence
>1hbmA (length=548) Species: 145262 (Methanothermobacter thermautotrophicus) [Search protein sequence]
ADKLFINALKKKFEESPEEKKTTFYTLGGWKQSERKTEFVNAGKEVAAKR
GIPQYNPDIGTPLGQRVLMPYQVSTTDTYVEGDDLHFVNNAAMQQMWDDI
RRTVIVGLNHAHAVIEKRLGKEVTPETITHYLETVNHAMPGAAVVQEHMV
ETHPALVADSYVKVFTGNDEIADEIDPAFVIDINKQFPEDQAETLKAEVG
DGIWQVVRIPTIVSRTCDGATTSRWSAMQIGMSMISAYKQAAGEAATGDF
AYAAKHAEVIHMGTYLPVRRARGENEPGGVPFGYLADICQSSRVNYEDPV
RVSLDVVATGAMLYDQIWLGSYMSGGVGFTQYATAAYTDNILDDFTYFGK
EYVEDKYGLCEAPNNMDTVLDVATEVTFYGLEQYEEYPALLEDQFGGSQR
AAVVAAAAGCSTAFATGNAQTGLSGWYLSMYLHKEQHSRLGFYGYDLQDQ
CGASNVFSIRGDEGLPLELRGPNYPNYAMNVGHQGEYAGISQAPHAARGD
AFVFNPLVKIAFADDNLVFDFTNVRGEFAKGALREFEPAGERALITPA
3D structure
PDB1hbm On the Mechanism of Biological Methane Formation: Structural Evidence for Conformational Changes in Methyl-Coenzyme M Reductase Upon Substrate Binding
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q147 Y333 G445 N481
Catalytic site (residue number reindexed from 1) Q146 Y332 G444 N480
Enzyme Commision number 2.8.4.1: coenzyme-B sulfoethylthiotransferase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0046872 metal ion binding
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:1hbm, PDBe:1hbm, PDBj:1hbm
PDBsum1hbm
PubMed11491299
UniProtP11558|MCRA_METTM Methyl-coenzyme M reductase I subunit alpha (Gene Name=mcrA)

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