Structure of PDB 1n63 Chain E

Receptor sequence
>1n63E (length=795) Species: 504832 (Afipia carboxidovorans OM5) [Search protein sequence]
AEKLQGMGCKRKRVEDIRFTQGKGNYVDDVKLPGMLFGDFVRSSHAHARI
KSIDTSKAKALPGVFAVLTAADLKPLNLHYMPTLAGDVQAVLADEKVLFQ
NQEVAFVVAKDRYVAADAIELVEVDYEPLPVLVDPFKAMEPDAPLLREDI
KDKMTGAHGARKHHNHIFRWEIGDKEGTDATFAKAEVVSKDMFTYHRVHP
SPLETCQCVASMDKIKGELTLWGTFQAPHVIRTVVSLISGLPEHKIHVIA
PDIGGGFGNKVGAYSGYVCAVVASIVLGVPVKWVEDRMENLSTTSFARDY
HMTTELAATKDGKILAMRCHVLADHGAFDACADPSKWPAGFMNICTGSYD
MPVAHLAVDGVYTNKASGGVAYRCSFRVTEAVYAIERAIETLAQRLEMDS
ADLRIKNFIQPEQFPYMAPLGWEYDSGNYPLAMKKAMDTVGYHQLRAEQK
AKQEAFKRGETREIMGIGISFFTEIVGAGPSKNCDILGVSMFDSAEIRIH
PTGSVIARMGTKSQGQGHETTYAQIIATELGIPADDIMIEEGNTDTAPYG
LGTYGSRSTPTAGAATAVAARKIKAKAQMIAAHMLEVHEGDLEWDVDRFR
VKGLPEKFKTMKELAWASYNSPPPNLEPGLEAVNYYDPPNMTYPFGAYFC
IMDIDVDTGVAKTRRFYALDDCGTRINPMIIEGQVHGGLTEAFAVAMGQE
IRYDEQGNVLGASFMDFFLPTAVETPKWETDYTVTPSPHHPIGAKGVGES
PHVGGVPCFSNAVNDAYAFLNAGHIQMPHDAWRLWKVGEQLGLHV
3D structure
PDB1n63 Catalysis at a dinuclear [CuSMo(=O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution
ChainE
Resolution1.21 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q240 V275 P352 I358 R387 C388 E763 S764
Catalytic site (residue number reindexed from 1) Q226 V261 P338 I344 R373 C374 E749 S750
Enzyme Commision number 1.2.5.3: aerobic carbon monoxide dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0005507 copper ion binding
GO:0008805 carbon-monoxide oxygenase activity
GO:0016491 oxidoreductase activity
GO:0030151 molybdenum ion binding
GO:0043885 anaerobic carbon-monoxide dehydrogenase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:1n63, PDBe:1n63, PDBj:1n63
PDBsum1n63
PubMed12475995
UniProtP19919|DCML_AFIC5 Carbon monoxide dehydrogenase large chain (Gene Name=coxL)

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