Structure of PDB 1gtt Chain C

Receptor sequence
>1gttC (length=421) Species: 562 (Escherichia coli) [Search protein sequence]
MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIGCGE
PIPFPQGEKVLSGATVALIVGKTATKVREEDAAEYIAGYALANDVSLPEE
SFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTADLQ
RNAAQLLSALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLE
NPVVDEREVTTRKSFPTLPHPHGTLFALGLNYADHPEEPLVFLKAPNTLT
GDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVAGYTVCNDY
AIRDYLENYYRPNLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGE
LRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLSDVVPGDEV
VVEVEGVGRLVNRIVSEETAK
3D structure
PDB1gtt The Crystal Structure of Hpce, a Bifunctional Decarboxylase/Isomerase with a Multifunctional Fold.
ChainC
Resolution1.7 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 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 C 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1gtt, PDBe:1gtt, PDBj:1gtt
PDBsum1gtt
PubMed11863436
UniProtP37352|HPCE_ECOLX Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase (Gene Name=hpcE)

[Back to BioLiP]