› 3nxp

X-ray diffraction
2.2Å resolution

Crystal structure of human prethrombin-1

Released:
DOI: 10.2210/pdb3nxp/pdb
PDB entry 3nxp coloured by chain, front view.
PDB entry 3nxp coloured by chain, side view.
PDB entry 3nxp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of prethrombin-1.
Chen Z, Pelc LA, Di Cera E
Proc Natl Acad Sci U S A 107 19278-83 (2010)
PMID: 20974933

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prothrombin Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 47.84 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P00734 (Residues: 199-622; Coverage: 71%)
Gene name: F2
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NAG 1 x NAG
Ligand TRS 2 x TRS
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 67.893Å b: 81.006Å c: 88.463Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.198 0.226
Expression system: Cricetulus griseus

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Citations

4 review citations

Conformational selection in trypsin-like proteases.
Pozzi et al. (2012)
3 more

9 mentions without citation

Allostery in trypsin-like proteases suggests new therapeutic strategies.
Gohara et al. (2011)
8 more