Structure of PDB 1e6v Chain E

Receptor sequence
>1e6vE (length=436) Species: 2320 (Methanopyrus kandleri) [Search protein sequence]
DTVDLYDDRGNCVAEEVPIEVLSPMRNEAIQSIVNDIKRTVAVDLEGIEN
ALQNATVGGKGMKIPGREMDVDIVDNAEAIADEIEKMIRVYQDDDTNVEP
MYDGKRLLVQLPSERVKVMADPYSGTLQAGMAVVHAIIDVCEVDMWDANM
VKAAVFGRYPQTIDYFGGNVASMLDVPMKQEGVGYALRNIMVNHIVAATR
KNTMQAVCLAATLQQTAMFEMGDALGPFERLHLLGYAYQGLNADNMVYDI
VKKHGKEGTVGTVVREVVERALEDGVIEVKEELPSFKVYKANDMDLWNAY
AAAGLVAAVMVNQGAARAAQGVSATILYYNDLLEYETGLPGVDFGRAEGT
AVGFSFFSHSIYGGGGPGIFHGNHIVTRHSKGFAIPPVAAAMALDAGTQM
FSPEVTSKLIGDVFGEIDEFREPMKYITEAAAEEAK
3D structure
PDB1e6v Comparison of Three Methyl-Coenzyme M Reductases from Phylogenetically Distant Organisms: Unusual Amino Acid Modification, Conservation and Adaptation
ChainE
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y368
Catalytic site (residue number reindexed from 1) Y362
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 I367 Y368 I361 Y362
BS02 TP7 E Y368 G370 Y362 G364
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0050524 coenzyme-B sulfoethylthiotransferase activity
Biological Process
GO:0015948 methanogenesis

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1e6v, PDBe:1e6v, PDBj:1e6v
PDBsum1e6v
PubMed11023796
UniProtQ49601

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