Structure of PDB 2vl1 Chain A Binding Site BS03

Receptor Information

>2vl1 Chain A (length=433) Species: 4934 (Lachancea kluyveri) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

PLSIASGRLNQTILETGSQFGGVARWGQESHEFGMRRLAGTALDGAMRDW
FTNECESLGCKVKVDKIGNMFAVYPGKNGGKPTATGSHLDTQPEAGKYDG
ILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSH
DLSLEEAYGLMSVGEDKPESVYDSLKNIGYIGDTPASYKENEIDAHFELH
IEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALL
MSSKMIVAASEIAQRHNGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSD
DVLATMLKEAAAEFDRLIKINDGGALSYESETLQVSPAVNFHEVCIECVS
RSAFAQFKKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEY
SSPEEIENGFKVLLQAIINYDNYRVIRGHQFPG

Ligand information

Ligand ID

InChI

InChI=1S/Zn/q+2

InChIKey

PTFCDOFLOPIGGS-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.341	[Zn++]
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Zn+2]

Formula

Name

ZINC ION

PDB chain

2vl1 Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2vl1 A Recruited Protease is Involved in Catabolism of Pyrimidines.
Resolution	2.15 Å
Binding residue (original residue number in PDB)	H114 D125 H226
Binding residue (residue number reindexed from 1)	H88 D99 H200
Annotation score	1

Enzymatic activity

Enzyme Commision number

3.5.1.6: beta-ureidopropionase.

Gene Ontology

	Molecular Function
GO:0003837	beta-ureidopropionase activity
GO:0016787	hydrolase activity
GO:0016813	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872	metal ion binding

View graph for
Molecular Function

External links

PDB	RCSB:2vl1, PDBe:2vl1, PDBj:2vl1
PDBsum	2vl1
PubMed	18448119
UniProt	Q96W94

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