Structure of PDB 1i7o Chain D

Receptor sequence
>1i7oD (length=421) Species: 562 (Escherichia coli) [Search protein sequence]
MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIGCGE
PIPFPQGEKVLSGATVALIVGKTATKVREEDAAEYIAGYALANDVSLPEE
SFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTADLQ
RNAAQLLSALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLE
NPVVDEREVTTRKSFPTLPHPHGTLFALGLNYADHPEEPLVFLKAPNTLT
GDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVAGYTVCNDY
AIRDYLENYYRPNLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGE
LRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLSDVVPGDEV
VVEVEGVGRLVNRIVSEETAK
3D structure
PDB1i7o The crystal structure of HpcE, a multi-functional enzyme fold
ChainD
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.68: 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase.
5.3.3.10: 5-carboxymethyl-2-hydroxymuconate Delta-isomerase.
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 CA D E276 E278 D307 E268 E270 D299
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008704 5-carboxymethyl-2-hydroxymuconate delta-isomerase activity
GO:0016829 lyase activity
GO:0016853 isomerase activity
GO:0018773 acetylpyruvate hydrolase activity
GO:0018800 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase activity
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process
GO:1901023 4-hydroxyphenylacetate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1i7o, PDBe:1i7o, PDBj:1i7o
PDBsum1i7o
PubMed
UniProtP37352|HPCE_ECOLX Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase (Gene Name=hpcE)

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