› 1mu8

X-ray diffraction
2Å resolution

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 domain:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133091 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain Chain: A
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 328-363; Coverage: 6%)
Gene name: F2
Sequence domains: Thrombin light chain
Thrombin heavy chain Chain: B
Molecule details ›
Chain: B
Length: 259 amino acids
Theoretical weight: 29.78 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Hirudin-2B Chain: C
Molecule details ›
Chain: C
Length: 11 amino acids
Theoretical weight: 1.49 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
  • Canonical: P28506 (Residues: 55-65; Coverage: 17%)

Ligands and Environments

1 bound ligand:
Ligand CDB 1 x CDB
1 modified residue:
Ligand TYS 1 x TYS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 71.12Å b: 72.23Å c: 73.03Å
α: 90° β: 100.8° γ: 90°
R-values:
R R work R free
0.209 0.24 not available
Expression system: Not provided

Quick links

Citations

5 review citations

Heterocyclic N-Oxides - An Emerging Class of Therapeutic Agents.
Mfuh et al. (2015)
4 more

2 mentions without citation

Enhanced ligand sampling for relative protein-ligand binding free energy calculations.
Kaus et al. (2015)
1 more