PDBe 4rkj

X-ray diffraction
1.7Å resolution

Crystal structure of thrombin mutant S195T (free form)

Released:
Source organism: Homo sapiens
Primary publication:
Why ser and not thr brokers catalysis in the trypsin fold.
Biochemistry 54 1457-64 (2015)
PMID: 25664608

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

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin light chain Chain: A
Molecule details ›
Chain: A
Length: 34 amino acids
Theoretical weight: 3.85 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P00734 (Residues: 330-363; Coverage: 6%)
Gene name: F2
Thrombin heavy chain Chain: B
Molecule details ›
Chain: B
Length: 259 amino acids
Theoretical weight: 29.79 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21212
Unit cell:
a: 61.415Å b: 91.114Å c: 50.553Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.156 0.207
Expression system: Cricetulus griseus