Structure of PDB 1q7l Chain C Binding Site BS03

Receptor Information
>1q7l Chain C (length=190) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPG
YVVTVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIY
ARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMEL
FVQRPEFHALRAGFALDEGIANPTDAFTVFYSERSPWWVR
Ligand information
Ligand IDGLY
InChIInChI=1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)
InChIKeyDHMQDGOQFOQNFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C(=O)O)N
CACTVS 3.341NCC(O)=O
ACDLabs 10.04O=C(O)CN
FormulaC2 H5 N O2
NameGLYCINE
ChEMBLCHEMBL773
DrugBankDB00145
ZINCZINC000004658552
PDB chain1q7l Chain C Residue 902 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1q7l Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family.
Resolution1.4 Å
Binding residue
(original residue number in PDB)		D113 E147 E148 E175
Binding residue
(residue number reindexed from 1)		D106 E140 E141 E168
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.14: N-acyl-aliphatic-L-amino acid amidohydrolase.
Gene Ontology
Molecular Function
GO:0004046 aminoacylase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006520 amino acid metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1q7l, PDBe:1q7l, PDBj:1q7l
PDBsum1q7l
PubMed12933810
UniProtQ03154|ACY1_HUMAN Aminoacylase-1 (Gene Name=ACY1)

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