› 3osl

X-ray diffraction
6Å resolution

Structure of bovine thrombin-activatable fibrinolysis inhibitor in complex with tick carboxypeptidase inhibitor

Released:
DOI: 10.2210/pdb3osl/pdb
PDB entry 3osl coloured by chain, front view.
PDB entry 3osl coloured by chain, side view.
PDB entry 3osl coloured by chain, top view.
Source organisms:
Primary publication:
Flexibility of the thrombin-activatable fibrinolysis inhibitor pro-domain enables productive binding of protein substrates.
Valnickova Z, Sanglas L, Arolas JL, Petersen SV, Schar C, Otzen D, Aviles FX, Gomis-Rüth FX, Enghild JJ
J Biol Chem 285 38243-50 (2010)
PMID: 20880845

Function and Biology Details

Reaction catalysed: 
Release of C-terminal Arg and Lys from a polypeptide.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173690 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carboxypeptidase B2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 401 amino acids
Theoretical weight: 46.53 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q2KIG3 (Residues: 23-423; Coverage: 100%)
Gene name: CPB2
Sequence domains:
Carboxypeptidase inhibitor Chains: B, D
Molecule details ›
Chains: B, D
Length: 74 amino acids
Theoretical weight: 7.81 KDa
Source organism: Rhipicephalus bursa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5EPH2 (Residues: 23-96; Coverage: 99%)
Sequence domains: Carboxypeptidase inhibitor I68

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P4132
Unit cell:
a: 279.1Å b: 279.1Å c: 279.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.313 0.313 0.32
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Structure-function relationships in thrombin-activatable fibrinolysis inhibitor.
Plug et al. (2016)
1 more

1 mention without citation

Flexibility of the thrombin-activatable fibrinolysis inhibitor pro-domain enables productive binding of protein substrates.
Valnickova et al. (2010)