Structure of PDB 2oof Chain A Binding Site BS01
Receptor Information
>2oof Chain A (length=403) Species:
32644
(unidentified) [
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LNCERVWLNVTPATLRSDLADYGLLEPHALGVHEGRIHALVPMQDLKYPA
HWQDMKGKLVTPGLIDCHTHLIFAGSRAEEFELRQKGVPYAEIARKGGGI
ISTVRATRAASEDQLFELALPRVKSLIREGVTTVEIKSGYGLTLEDELKM
LRVARRLGEALPIRVKTTLLAAHAVPPEYRDDPDSWVETICQEIIPAAAE
AGLADAVDVFCEHIGFSLAQTEQVYLAADQYGLAVKGHMDQLSNLGGSTL
AANFGALSVDHLEYLDPEGIQALAHRGVVATLLPTAFYFLKETKLPPVVA
LRKAGVPMAVSSDINPGTAPIVSLRMAMNMACTLFGLTPVEAMAGVTRHA
ARALGEQEQLGQLRVGMLADFLVWNCGHPAELSYLIGVDQLVSRVVNGEE
TLH
Ligand information
Ligand ID
FE
InChI
InChI=1S/Fe/q+3
InChIKey
VTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
Formula
Fe
Name
FE (III) ION
ChEMBL
DrugBank
DB13949
ZINC
PDB chain
2oof Chain A Residue 500 [
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Receptor-Ligand Complex Structure
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PDB
2oof
The crystal structure of 4-imidazolone-5-propanoate amidohydrolase from environmental sample
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
H72 H74 H242 D317
Binding residue
(residue number reindexed from 1)
H68 H70 H238 D313
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.5.2.7
: imidazolonepropionase.
Gene Ontology
Molecular Function
GO:0005506
iron ion binding
GO:0008270
zinc ion binding
GO:0016787
hydrolase activity
GO:0016810
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0016812
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
GO:0046872
metal ion binding
GO:0050480
imidazolonepropionase activity
Biological Process
GO:0006547
L-histidine metabolic process
GO:0006548
L-histidine catabolic process
GO:0019556
L-histidine catabolic process to glutamate and formamide
GO:0019557
L-histidine catabolic process to glutamate and formate
Cellular Component
GO:0005737
cytoplasm
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2oof
,
PDBe:2oof
,
PDBj:2oof
PDBsum
2oof
PubMed
UniProt
A0KF84
|HUTI_AERHH Imidazolonepropionase (Gene Name=hutI)
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