Structure of PDB 5n1q Chain D

Receptor sequence
>5n1qD (length=549) Species: 523845 (Methanothermococcus thermolithotrophicus DSM 2095) [Search protein sequence]
KKLFLKALKEKFEEDPKEKYTKFYTFGGWQQSARKREFVEANEKIVAEKR
GGIPMYNPDIGVPLGQRKLMPYKLSGTDYIVEGDDLHFMNNAAIQQMWDD
IRRTVIVGMDTGHAVLEKRLGVEVTPETINEYMATINHSLPGGAVVQEHM
VEVHPSLAWDCYAKIFTGDDELADELDKKYLIDINKLFPEEQAEQLKAAI
GKKTYQVSRVPTLVGRVCDGGTIARWSAMQIGMSFITAYKLCAGEAAIAD
FSYAAKHADVVGVGTALPARRSRGANEPGGIPFGVLCDIVQTTRISDDPV
EQSLEVVAVGAMLYDQVWLGSYMSGGVGFTQYATAAYTDDILDDFAYYGY
EYVEKKYGINSTKPTMDVVEDIATEVTLYSLEQYDEFPTLLEDHFGGSQR
AAVAAAASGISVCMATGNSNAGVNGWYLSQIMHKEYHSRLGFYGYDLQDQ
CGASNSLSIRNDEASPLELRGPNYPNYAMNVGHQGEYAGITQAAHSARKD
AFAMNPLIKIAFADPSLVFDFARPRKECARGALREFEAAGERDVILPAK
3D structure
PDB5n1q Phylogenetic and Structural Comparisons of the Three Types of Methyl Coenzyme M Reductase from Methanococcales and Methanobacteriales.
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y336 G448 N484
Catalytic site (residue number reindexed from 1) 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:5n1q, PDBe:5n1q, PDBj:5n1q
PDBsum5n1q
PubMed28559298
UniProtA0A247D6X3

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