Structure of PDB 2boa Chain B

Receptor sequence

>2boaB (length=404) Species: 9606 (Homo sapiens)

REKFFGDQVLRINVRNGDEISKLSQLVNSNNLKLNFWKSPSSFNRPVDVL
VPSVSLQAFKSFLRSQGLEYAVTIEDLQALLDNEDDEMQHNEGQERSSNN
FNYGAYHSLEAIYHEMDNIAADFPDLARRVKIGHSFENRPMYVLKFSTGK
GVRRPAVWLNAGIHSREWISQATAIWTARKIVSDYQRDPAITSILEKMDI
FLLPVANPDGYVYTQTQNRLWRKTRSRNPGSSCIGADPNRNWNASFAGKG
ASDNPCSEVYHGPHANSEVEVKSVVDFIQKHGNFKGFIDLHSYSQLLMYP
YGYSVKKAPDAEELDKVARLAAKALASVSGTEYQVGPTCTTVYPASGSSI
DWAYDNGIKFAFTFELRDTGTYGFLLPANQIIPTAEETWLGLKTIMEHVR
DNLY

3D structure

• PDB: 2boa Detailed Molecular Comparison between the Inhibition Mode of A/B-Type Carboxypeptidases in the Zymogen State and by the Endogenous Inhibitor Latexin.
• Chain: B
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H1069 E1072 R1127 H1196 E1270
• Catalytic site (residue number reindexed from 1): H164 E167 R222 H291 E365
• Enzyme Commision number: 3.4.17.-

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	B	H1069 E1072 H1196	H164 E167 H291

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:0042447 hormone catabolic process
• GO:0043171 peptide catabolic process

Cellular Component

• GO:0005575 cellular_component
• GO:0005576 extracellular region
• GO:0005615 extracellular space

External links

• PDB: RCSB:2boa, PDBe:2boa, PDBj:2boa
• PDBsum: 2boa
• PubMed: 16091843
• UniProt: Q9UI42|CBPA4_HUMAN Carboxypeptidase A4 (Gene Name=CPA4)