Structure of PDB 8dqc Chain A

Receptor sequence
>8dqcA (length=361) Species: 571 (Klebsiella oxytoca) [Search protein sequence]
HHMQDEMYMARALKLAARGRFTTHPNPNVGCVIVKDGEIVGEGFHYRAGE
PHAEVHALRMAGDKAKGATAYVTLEPCPPCCDALIAAGVARVVAAMQDPN
VAGRGLYRLQQAGIDVSHGLMMNEAEALNKGFLKRMRTGFPWIQLKMGAS
LDGRTAMASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTV
RWQELSADTQALYPQENLRQPLRIVIDSQNRVTPEHRIIQQQGETLFART
HADERAWPDNVRTLLVPEHNGHLDLVLLMMQLGKQQVNSIWVEAGPTLAG
ALLQAGLVDELIVYIAPKLLGSDARGLCALPGLEKLSQAPHFKFNEIRQV
GPDVCLHLTTA
3D structure
PDB8dqc Crystal structure of 3-dehydroquinate dehydratase I from Klebsiella oxytoca (I222 Form)
ChainA
Resolution2.7 Å
3D
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
Enzyme Commision number 1.1.1.193: 5-amino-6-(5-phosphoribosylamino)uracil reductase.
3.5.4.26: diaminohydroxyphosphoribosylaminopyrimidine deaminase.
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 ZN A H58 C83 C92 H52 C77 C80
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008270 zinc ion binding
GO:0008703 5-amino-6-(5-phosphoribosylamino)uracil reductase activity
GO:0008835 diaminohydroxyphosphoribosylaminopyrimidine deaminase activity
GO:0016491 oxidoreductase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0050661 NADP binding
Biological Process
GO:0009231 riboflavin biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:8dqc, PDBe:8dqc, PDBj:8dqc
PDBsum8dqc
PubMed
UniProtA0A0H3FX83

[Back to BioLiP]