Structure of PDB 3dgv Chain C

Receptor sequence

>3dgvC (length=379) Species: 9913 (Bos taurus)

QRGQVRTSRQVQILQNVTTTYKIVLWQPVAAEYEVHFFVNASDVSNVKAH
LNASIPFRVLVENVEDLIRQQTSSPRASSSYYEQYHSLNEIYSWIEVMTE
RYPDMVEKIHIGSSYEKYPLYVLKVSKKEKNAMWIDCGIHAREWISPAFC
LWFVGSVTYYYGKEKMHTNLLKHMDFYIMPVVNVDGYDYTWKKDRMWRKN
RSLHEKNACVGTDLNRNFASKHWCGEGASSSSCSEIYCGTYPESEPEVKA
VADFLRRNIKHIKAYISMHSYSQKIVFPYSYSRSRSKDHEELSLVAREAV
FAMENIHRNTHGSGSESLYLAPGGSDDWIYDLGIKYSFTFELRDKGKYGF
LLPESYIRPTCSEALVAVAKIASHVVKNV

3D structure

• PDB: 3dgv The crystal structure of thrombin-activable fibrinolysis inhibitor (TAFI) provides the structural basis for its intrinsic activity and the short half-life of TAFIa.
• Chain: C
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H69 E72 R127 H196 E270
• Catalytic site (residue number reindexed from 1): H140 E143 R198 H269 E341
• Enzyme Commision number: 3.4.17.20: carboxypeptidase U.

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	C	H69 E72 H196	H140 E143 H269

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:0007596 blood coagulation
• GO:0042730 fibrinolysis

Cellular Component

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

External links

• PDB: RCSB:3dgv, PDBe:3dgv, PDBj:3dgv
• PDBsum: 3dgv
• PubMed: 18669641
• UniProt: Q2KIG3|CBPB2_BOVIN Carboxypeptidase B2 (Gene Name=CPB2)