Structure of PDB 1mjg Chain M

Receptor sequence
>1mjgM (length=728) Species: 1525 (Moorella thermoacetica) [Search protein sequence]
TDFDKIFEGAIPEGKEPVALFREVYHGAITATSYAEILLNQAIRTYGPDH
PVGYPDTAYYLPVIRCFSGEEVKKLGDLPPILNRKRAQVSPVLNFENARL
AGEATWYAAEIIEALRYLKYKPDEPLLPPPWTGFIGDPVVRRFGIKMVDW
TIPGEAIILGRAKDSKALAKIVKELMGMGFMLFICDEAVEQLLEENVKLG
IDYIAYPLGNFTQIVHAANYALRAGMMFGGVTPGAREEQRDYQRRRIRAF
VLYLGEHDMVKTAAAFGAIFTGFPVITDQPLPEDKQIPDWFFSVEDYDKI
VQIAMETRGIKLTKIKLDLPINFGPAFEGESIRKGDMYVEMGGNRTPAFE
LVRTVSESEITDGKIEVIGPDIDQIPEGSKLPLGILVDIYGRKMQADFEG
VLERRIHDFINYGEGLWHTGQRNINWLRVSKDAVAKGFRFKNYGEILVAK
MKEEFPAIVDRVQVTIFTDEAKVKEYMEVAREKYKERDDRMRGLTDETVD
TFYSCVLCQSFAPNHVCIVTPERVGLCGAVSWLDAKASYEINHAGPNQPI
PKEGEIDPIKGIWKSVNDYLYTASNRNLEQVCLYTLMENPMTSCGCFEAI
MAILPECNGIMITTRDHAGMTPSGMTFSTLAGMIGGGTQTPGFMGIGRTY
IVSKKFISADGGIARIVWMPKSLKDFLHDEFVRSSVEEGLGEDFIDKIAD
ETIGTTVDEILPYLEEKGHPALTMDPIM
3D structure
PDB1mjg A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase
ChainM
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.169: CO-methylating acetyl-CoA synthase.
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 CU1 M C509 C595 C597 C508 C594 C596
BS02 SF4 M I146 C506 L508 C509 C518 L527 C528 V531 I145 C505 L507 C508 C517 L526 C527 V530
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016491 oxidoreductase activity
GO:0016740 transferase activity
GO:0043884 CO-methylating acetyl-CoA synthase activity
GO:0043885 anaerobic carbon-monoxide dehydrogenase activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006084 acetyl-CoA metabolic process
GO:0015977 carbon fixation

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Molecular Function
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Biological Process
External links
PDB RCSB:1mjg, PDBe:1mjg, PDBj:1mjg
PDBsum1mjg
PubMed12386327
UniProtP27988|DCMA_MOOTH Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha

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