Structure of PDB 1r3n Chain B Binding Site BS02

Receptor Information

>1r3n Chain B (length=433) Species: 4934 (Lachancea kluyveri) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

PAAAPLSIASGRLNQTILETGSQFGGVARWGQESHEFGMRRLAGTALDGA
MRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPTATGSHLDTQPEAG
KYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSS
VWSHDLSLEEAYGLMSVGEDKPESVYDSLKNIGYIGDTPASYKENEIDAH
FELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRK
DALLMSSKMIVAASEIAQRHNGLFTCGIIDAKPYSVNIIPGEVSFTLDFR
HPSDDVLATMLKEAAAEFDRLIKINDGGALSYESETLQVSPAVNFHEVCI
ECVSRSAFAQFKKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHN
YYEYSSPEEIENGFKVLLQAIINYDNYRVIRGH

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

1r3n Chain B 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	1r3n Yeast beta-Alanine Synthase Shares a Structural Scaffold and Origin with Dizinc-dependent Exopeptidases
Resolution	2.7 Å
Binding residue (original residue number in PDB)	H114 D125 H226
Binding residue (residue number reindexed from 1)	H92 D103 H204
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

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Molecular Function

External links

PDB	RCSB:1r3n, PDBe:1r3n, PDBj:1r3n
PDBsum	1r3n
PubMed	14534321
UniProt	Q96W94

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