1mkx

X-ray diffraction
2.2Å resolution

THE CO-CRYSTAL STRUCTURE OF UNLIGANDED BOVINE ALPHA-THROMBIN AND PRETHROMBIN-2: MOVEMENT OF THE YPPW SEGMENT AND ACTIVE SITE RESIDUES UPON LIGAND BINDING

Released:

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:

Structure analysis Details

Assemblies composition:
hetero dimer
monomeric
hetero hexamer (preferred)
homo dimer
hetero tetramer
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain Chain: L
Molecule details ›
Chain: L
Length: 49 amino acids
Theoretical weight: 5.74 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00735 (Residues: 318-366; Coverage: 8%)
Gene name: F2
Sequence domains: Thrombin light chain
Thrombin heavy chain Chain: H
Molecule details ›
Chain: H
Length: 259 amino acids
Theoretical weight: 29.77 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00735 (Residues: 367-625; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Thrombin heavy chain Chain: K
Molecule details ›
Chain: K
Length: 308 amino acids
Theoretical weight: 35.49 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00735 (Residues: 318-625; Coverage: 51%)
Gene name: F2
Sequence domains:
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 87.52Å b: 87.99Å c: 101.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.255