Structure of PDB 1aye Chain A Binding Site BS01

Receptor Information
>1aye Chain A (length=401) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LETFVGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSPTTPGETAHVR
VPFVNVQAVKVFLESQGIAYSIMIEDVQVLLDKENEEMLFNRRRERSGNF
NFGAYHTLEEISQEMDNLVAEHPGLVSKVNIGSSFENRPMNVLKFSTGGD
KPAIWLDAGIHAREWVTQATALWTANKIVSDYGKDPSITSILDALDIFLL
PVTNPDGYVFSQTKNRMWRKTRSKVSGSLCVGVDPNRNWDAGFGGPGASS
NPCSDSYHGPSANSEVEVKSIVDFIKSHGKVKAFIILHSYSQLLMFPYGY
KCTKLDDFDELSEVAQKAAQSLRSLHGTKYKVGPICSVIYQASGGSIDWS
YDYGIKYSFAFELRDTGRYGFLLPARQILPTAEETWLGLKAIMEHVRDHP
Y
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 chain1aye Chain A Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1aye The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		H69 E72 H196
Binding residue
(residue number reindexed from 1)		H161 E164 H288
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H69 E72 R127 H196 E270
Catalytic site (residue number reindexed from 1) H161 E164 R219 H288 E362
Enzyme Commision number 3.4.17.15: carboxypeptidase A2.
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0004181 metallocarboxypeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0007039 protein catabolic process in the vacuole
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005773 vacuole

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1aye, PDBe:1aye, PDBj:1aye
PDBsum1aye
PubMed9384570
UniProtP48052|CBPA2_HUMAN Carboxypeptidase A2 (Gene Name=CPA2)

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