Structure of PDB 5tp4 Chain A Binding Site BS01

Receptor Information
>5tp4 Chain A (length=405) Species: 398577 (Burkholderia ambifaria MC40-6) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLLEIDGARLWRSLADMARIGATPRGGVRRLALTDDDRRGRDLFAQWCRD
AGMTVSVDAVGNLFARRDGADAQAAPVLIGSHLDTQPEGGRFDGVYGVLA
GLEVVRTLNDAGIVTDKPLEIVSWTNEEGARFAPAMLGSAVFTGALPLDD
ALARQDAEGITLGAALDACGCRGTRAPGGAVDAYFEAHIEQGPVLEANGT
TIGIVTGGQAIRWLDVRVTGVAAHAGTTPMPYRKDAYFASAQMALELERI
VAGHAPRGLATIGQAGIRNASRNTIAGDVTFTVDLRHHDDAQVDAMERAL
RDACARVAAARGVQVAIDTCWRSPATPFDRGCVELVARAAEAFGYTNERI
VSGAGHDAILLARRVPTAMVFIPCVDAEDALPDDVTRGTNVLLNAVLARA
GVATR
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5tp4 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5tp4 Crystal structure of a hydantoinase/carbamoylase family amidase from Burkholderia ambifaria
Resolution1.7 Å
Binding residue
(original residue number in PDB)
H84 H190
Binding residue
(residue number reindexed from 1)
H82 H188
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.87: N-carbamoyl-L-amino-acid hydrolase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872 metal ion binding
GO:0050538 N-carbamoyl-L-amino-acid hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:5tp4, PDBe:5tp4, PDBj:5tp4
PDBsum5tp4
PubMed
UniProtB1YW99

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