Structure of PDB 1kwm Chain A

Receptor sequence

>1kwmA (length=402) Species: 9606 (Homo sapiens)

HHGGEHFEGEKVFRVNVEDENHINIIRELASTTQIDFWKPDSVTQIKPHS
TVDFRVKAEDTVTVENVLKQNELQYKVLISNLRNVVEAQFDSRVRATGHS
YEKYNKWETIEAWTQQVATENPALISRSVIGTTFEGRAIYLLKVGKAGQN
KPAIFMDCGFHAREWISPAFCQWFVREAVRTYGREIQVTELLNKLDFYVL
PVLNIDGYIYTWTKSRFWRKTRSTHTGSSCIGTDPNRNFDAGWCEIGASR
NPCDETYCGPAAESEKETKALADFIRNKLSSIKAYLTIHSYSQMMIYPYS
YAYKLGENNAELNALAKATVKELASLHGTKYTYGPGATTIYPAAGGSDDW
AYDQGIRYSFTFELRDTGRYGFLLPESQIRATCEETFLAIKYVASYVLEH
LY

3D structure

• PDB: 1kwm Human procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI).
• Chain: A
• Resolution: 1.6 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 H289 E363
• Enzyme Commision number: 3.4.17.2: carboxypeptidase B.

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 H289

Gene Ontology

Molecular Function

• GO:0004180 carboxypeptidase activity
• GO:0004181 metallocarboxypeptidase activity
• GO:0005515 protein binding
• GO:0008237 metallopeptidase activity
• GO:0008270 zinc ion binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0005576 extracellular region
• GO:0005615 extracellular space
• GO:0031410 cytoplasmic vesicle

External links

• PDB: RCSB:1kwm, PDBe:1kwm, PDBj:1kwm
• PDBsum: 1kwm
• PubMed: 12162965
• UniProt: P15086|CBPB1_HUMAN Carboxypeptidase B (Gene Name=CPB1)