Structure of PDB 8dq9 Chain B

Receptor sequence
>8dq9B (length=364) Species: 571 (Klebsiella oxytoca) [Search protein sequence]
QDEMYMARALKLAARGRFTTHPNPNVGCVIVKDGEIVGEGFHYRAGEPHA
EVHALRMAGDKAKGATAYVTLEPCSHHTPPCCDALIAAGVARVVAAMQDP
NPQVAGRGLYRLQQAGIDVSHGLMMNEAEALNKGFLKRMRTGFPWIQLKM
GASLDGRTAMASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPA
LTVRWQELSADTQALYPQENLRQPLRIVIDSQNRVTPEHRIIQQQGETLF
ARTHADERAWPDNVRTLLVPEHNGHLDLVLLMMQLGKQQVNSIWVEAGPT
LAGALLQAGLVDELIVYIAPKLLGSDARGLCALPGLEKLSQAPHFKFNEI
RQVGPDVCLHLTTA
3D structure
PDB8dq9 Crystal structure of GDP bound 3-dehydroquinate dehydratase I from Klebsiella oxytoca
ChainB
Resolution2.8 Å
3D
structure
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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 B H58 C83 C92 H49 C74 C81
BS02 GDP B S201 S202 A203 S242 R245 H286 L289 T311 A315 S190 S191 A192 S231 R234 H275 L278 T300 A304
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

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Molecular Function
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Biological Process
External links
PDB RCSB:8dq9, PDBe:8dq9, PDBj:8dq9
PDBsum8dq9
PubMed
UniProtA0A0H3FX83

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