Structure of PDB 1e6y Chain A

Receptor sequence
>1e6yA (length=568) Species: 2208 (Methanosarcina barkeri) [Search protein sequence]
AADIFSKFKKDMEVKFAQEFGSNKQTGGDITDKTAKFLRLGPEQDPRKVE
MIKAGKEIAEKRGIAFYNPMMHSGAPLGQRAITPYTISGTDIVCEPDDLH
YVNNAAMQQMWDDIRRTCIVGLDMAHETLEKRLGKEVTPETINHYLEVLN
HAMPGAAVVQEMMVETHPALVDDCYVKVFTGDDALADEIDKQFLIDINKE
FSEEQAAQIKASIGKTSWQAIHIPTIVSRTTDGAQTSRWAAMQIGMSFIS
AYAMCAGEAAVADLSFAAKHAALVSMGEMLPARRARGPNEPGGLSFGHLS
DIVQTSRVSEDPAKIALEVVGAGCMLYDQIWLGSYMSGGVGFTQYATAAY
TDDILDNNTYYDVDYINDKYNGAATVGKDNKVKASLEVVKDIATESTLYG
IETYEKFPTALEDHFGGSQRATVLAAAAGVACSLATGNANAGLSGWYLSM
YLHKEAWGRLGFFGFDLQDQCGATNVLSYQGDEGLPDELRGPNYPNYAMN
VGHQGGYAGIAQAAHSGRGDAFTVNPLLKVCFADDLLPFNFAEPRREFGR
GAIREFVPAGERSLVIPA
3D structure
PDB1e6y Comparison of Three Methyl-Coenzyme M Reductases from Phylogenetically Distant Organisms: Unusual Amino Acid Modification, Conservation and Adaptation
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y1346 G1465 N1501
Catalytic site (residue number reindexed from 1) Y345 G464 N500
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:1e6y, PDBe:1e6y, PDBj:1e6y
PDBsum1e6y
PubMed11023796
UniProtP07962|MCRA_METBF Methyl-coenzyme M reductase subunit alpha (Gene Name=mcrA)

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