Structure of PDB 3osl Chain C

Receptor sequence
>3oslC (length=296) Species: 9913 (Bos taurus) [Search protein sequence]
SYYEQYHSLNEIYSWIEVMTERYPDMVEKIHIGSSYEKYPLYVLKVSKKN
AMWIDCGIHAREWISPAFCLWFVGSVTYYYGKNLLKHMDFYIMPVVNVDG
YDYTWKKDRMWRKNRSLHEKNACVGTDLNRNFASKHWCGEGASSSSCSEI
YCGTYPESEPEVKAVADFLRRNIKHIKAYISMHSYSQKIVFPYSYSRSRS
KDHEELSLVAREAVFAMENIHRNIRYTHGSGSESLYLAPGGSDDWIYDLG
IKYSFTFELRDKGKYGFLLPESYIRPTCSEALVAVAKIASHVVKNV
3D structure
PDB3osl Flexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein Substrates.
ChainC
Resolution6.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H181 E184 R239 H310 E385
Catalytic site (residue number reindexed from 1) H59 E62 R112 H183 E258
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 H181 E184 H310 H59 E62 H183
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3osl, PDBe:3osl, PDBj:3osl
PDBsum3osl
PubMed20880845
UniProtQ2KIG3|CBPB2_BOVIN Carboxypeptidase B2 (Gene Name=CPB2)

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