› 2jor

Solution NMR

NMR Solution Structure, Stability, and Interaction of the Recombinant Bovine Fibrinogen alphaC-Domain Fragment

Released:
DOI: 10.2210/pdb2jor/pdb
PDB entry 2jor coloured by chain, ensemble of 20 models, front view.
PDB entry 2jor coloured by chain, ensemble of 20 models, side view.
PDB entry 2jor coloured by chain, ensemble of 20 models, top view.
Source organism: Bos taurus
Primary publication:
NMR solution structure, stability, and interaction of the recombinant bovine fibrinogen alphaC-domain fragment.
Burton RA, Tsurupa G, Hantgan RR, Tjandra N, Medved L
Biochemistry 46 8550-60 (2007)
PMID: 17590019

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136030 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibrinogen alpha chain Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 8.97 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P02672 (Residues: 437-515; Coverage: 13%)
Gene name: FGA
Sequence domains: Fibrinogen alpha C domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Fibrin-based biomaterials: modulation of macroscopic properties through rational design at the molecular level.
Brown et al. (2014)
7 more

7 mentions without citation

Structure, stability, and interaction of the fibrin(ogen) alphaC-domains.
Tsurupa et al. (2009)
6 more