Structure of PDB 4o6r Chain C

Receptor sequence
>4o6rC (length=489) Species: 216591 (Burkholderia cenocepacia J2315) [Search protein sequence]
HMQTQLFIDGRFVDAVDRGTIDVLNPHDGSVITKIAAATAADVDLAVDAA
TRAFPAWSAMPAAERGRLLLRLADAIEANTEALAQLESLDTGHPIRDSRA
LDVPRTAACFRYFGGMADKLQGSVIPVDTGFLNYVQRAPIGVVGQIVPWN
FPLMFTSWKMGPALAAGNTVVLKPSEITPLSTLRIVELMAEVGFPAGVVN
IVPGYGHTAGQRLAEHPGVGKIAFTGSTATGRRIVEASQGNLKRVQLELG
GKGANIVFDDANLDAAINGAAWAIFHNQGQACIAGSRLVLHERIADAFLE
RFVALASSIRIGNPLDPNTEMGPLTSKQHLDRVLSYVDVAREQGGRVLTG
GSAPQDPALANGYYVRPTIVEAKHATDRVAQEEVFGPFVTVLRFGSDDEA
LAIANATEYGLGSGLWTNDLSRAHRMAARIDAGMCWINCYKRVNPGSPFG
GVGKSGYGREMGFEAMHDYTEARSVWVNVDGNVPPHFKR
3D structure
PDB4o6r Crystal Structure of a Putative Aldehyde Dehydrogenase from Burkholderia cenocepacia
ChainC
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N149 K172 E247 C281 E382 E459
Catalytic site (residue number reindexed from 1) N150 K173 E248 C282 E383 E460
Enzyme Commision number ?
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 AMP C I145 V146 K172 G205 G209 Q210 F223 G225 S226 T229 I146 V147 K173 G206 G210 Q211 F224 G226 S227 T230
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

View graph for
Molecular Function
External links
PDB RCSB:4o6r, PDBe:4o6r, PDBj:4o6r
PDBsum4o6r
PubMed
UniProtB4EJX1

[Back to BioLiP]