› 1bth

X-ray diffraction
2.3Å resolution

STRUCTURE OF THROMBIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR

Released:
DOI: 10.2210/pdb1bth/pdb
PDB entry 1bth coloured by chain, front view.
PDB entry 1bth coloured by chain, side view.
PDB entry 1bth coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin.
van de Locht A, Bode W, Huber R, Le Bonniec BF, Stone SR, Esmon CT, Stubbs MT
EMBO J 16 2977-84 (1997)
PMID: 9214615

Function and Biology Details

Reaction catalysed: 
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133062 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain Chains: J, L
Molecule details ›
Chains: J, L
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Bos taurus
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P00734 (Residues: 328-363; Coverage: 6%)
Gene name: F2
Sequence domains: Thrombin light chain
Thrombin heavy chain Chains: H, K
Molecule details ›
Chains: H, K
Length: 259 amino acids
Theoretical weight: 29.81 KDa
Source organism: Bos taurus
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 71.2Å b: 74.5Å c: 83.4Å
α: 90° β: 92.5° γ: 90°
R-values:
R R work R free
0.196 0.196 0.271
Expression system: Mesocricetus auratus

Quick links

Citations

9 review citations

Thrombin.
Di Cera E. (2008)
8 more

16 mentions without citation

Anchor residues in protein-protein interactions.
Rajamani et al. (2004)
15 more