Structure of PDB 6zeq Chain A Binding Site BS02

Receptor Information
>6zeq Chain A (length=301) Species: 510516 (Aspergillus oryzae RIB40) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AVTYPDSVQHNETVQNLIKSLDKKNFETVLQPFSEFHNRYYKSDNGKKSS
EWLQGKIQEIISASGAKGVTVEPFKHSFPQSSLIAKIPGKSDKTIVLGAH
QDSINLDSPSEGRAPGADDDGSGVVTILEAFRVLLTDEKVAAGEAPNTVE
FHFYAGEEGGLLGSQDIFEQYSQKSRDVKAMLQQDMTGYTKGTTDAGKPE
SIGIITDNVDENLTKFLKVIVDAYCTIPTVDSKCGYGCSDHASATKYGYP
AAFAFESAFGDDSPYIHSADDTIETVNFDHVLQHGRLTLGFAYELAFADS
L
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 chain6zeq Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6zeq The role of propeptide-mediated autoinhibition and intermolecular chaperone in the maturation of cognate catalytic domain in leucine aminopeptidase.
Resolution1.97 Å
Binding residue
(original residue number in PDB)		D195 E234 H343
Binding residue
(residue number reindexed from 1)		D119 E158 H267
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H176 D195 E233 E234 D261 H343
Catalytic site (residue number reindexed from 1) H100 D119 E157 E158 D185 H267
Enzyme Commision number 3.4.11.-
Gene Ontology
Molecular Function
GO:0008235 metalloexopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:6zeq, PDBe:6zeq, PDBj:6zeq
PDBsum6zeq
PubMed33989771
UniProtQ2U1F3|LAPA_ASPOR Leucine aminopeptidase A (Gene Name=lapA)

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