Structure of PDB 1aye Chain A

Receptor sequence

>1ayeA (length=401) Species: 9606 (Homo sapiens)

LETFVGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSPTTPGETAHVR
VPFVNVQAVKVFLESQGIAYSIMIEDVQVLLDKENEEMLFNRRRERSGNF
NFGAYHTLEEISQEMDNLVAEHPGLVSKVNIGSSFENRPMNVLKFSTGGD
KPAIWLDAGIHAREWVTQATALWTANKIVSDYGKDPSITSILDALDIFLL
PVTNPDGYVFSQTKNRMWRKTRSKVSGSLCVGVDPNRNWDAGFGGPGASS
NPCSDSYHGPSANSEVEVKSIVDFIKSHGKVKAFIILHSYSQLLMFPYGY
KCTKLDDFDELSEVAQKAAQSLRSLHGTKYKVGPICSVIYQASGGSIDWS
YDYGIKYSFAFELRDTGRYGFLLPARQILPTAEETWLGLKAIMEHVRDHP
Y

3D structure

• PDB: 1aye The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen.
• Chain: A
• Resolution: 1.8 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	H69 E72 H196	H161 E164 H288

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

External links

• PDB: RCSB:1aye, PDBe:1aye, PDBj:1aye
• PDBsum: 1aye
• PubMed: 9384570
• UniProt: P48052|CBPA2_HUMAN Carboxypeptidase A2 (Gene Name=CPA2)