Structure of PDB 1r3n Chain E Binding Site BS01
Receptor Information
>1r3n Chain E (length=433) Species:
4934
(Lachancea kluyveri) [
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PAAAPLSIASGRLNQTILETGSQFGGVARWGQESHEFGMRRLAGTALDGA
MRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPTATGSHLDTQPEAG
KYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSS
VWSHDLSLEEAYGLMSVGEDKPESVYDSLKNIGYIGDTPASYKENEIDAH
FELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRK
DALLMSSKMIVAASEIAQRHNGLFTCGIIDAKPYSVNIIPGEVSFTLDFR
HPSDDVLATMLKEAAAEFDRLIKINDGGALSYESETLQVSPAVNFHEVCI
ECVSRSAFAQFKKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHN
YYEYSSPEEIENGFKVLLQAIINYDNYRVIRGH
Ligand information
Ligand ID
ZN
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
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1r3n Chain E Residue 500 [
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Receptor-Ligand Complex Structure
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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
View graph for
Molecular Function
External links
PDB
RCSB:1r3n
,
PDBe:1r3n
,
PDBj:1r3n
PDBsum
1r3n
PubMed
14534321
UniProt
Q96W94
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