› 5edk

X-ray diffraction
3.21Å resolution

Crystal structure of prothrombin deletion mutant residues 146-167 ( Form II ).

Released:
DOI: 10.2210/pdb5edk/pdb
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PDB entry 5edk coloured by chain, front view.
PDB entry 5edk coloured by chain, side view.
PDB entry 5edk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
How the Linker Connecting the Two Kringles Influences Activation and Conformational Plasticity of Prothrombin.
Pozzi N, Chen Z, Di Cera E
J Biol Chem 291 6071-82 (2016)
PMID: 26763231

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
Macromolecules (2 distinct):
Prothrombin Chain: A
Molecule details ›
Chain: A
Length: 560 amino acids
Theoretical weight: 63.99 KDa
Source organism: Homo sapiens
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P00734 (Residues: 44-622; Coverage: 93%)
Gene name: F2
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 2 x NAG
Ligand MG 4 x MG
1 modified residue:
Ligand CGU 10 x CGU

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P41212
Unit cell:
a: 84.192Å b: 84.192Å c: 346.427Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.293 0.291 0.323
Expression system: Mesocricetus auratus

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Citations

4 review citations

Plasminogen Activator Inhibitor Type-1 as a Regulator of Fibrosis.
Rabieian et al. (2018)
3 more

2 mentions without citation

How the Linker Connecting the Two Kringles Influences Activation and Conformational Plasticity of Prothrombin.
Pozzi et al. (2016)
1 more

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