› 1jy3

X-ray diffraction
1.6Å resolution

Crystal Structure of the Central Region of Bovine Fibrinogen (E5 Fragment) at 1.4 Angstroms Resolution

Released:
DOI: 10.2210/pdb1jy3/pdb
PDB entry 1jy3 coloured by chain, front view.
PDB entry 1jy3 coloured by chain, side view.
PDB entry 1jy3 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution.
Madrazo J, Brown JH, Litvinovich S, Dominguez R, Yakovlev S, Medved L, Cohen C
Proc Natl Acad Sci U S A 98 11967-72 (2001)
PMID: 11593005

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-136031 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Fibrinogen alpha chain Chains: N, Q
Molecule details ›
Chains: N, Q
Length: 53 amino acids
Theoretical weight: 6.17 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P02672 (Residues: 48-100; Coverage: 9%)
Gene name: FGA
Sequence domains: Fibrinogen alpha/beta chain family
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Fibrinogen beta chain Chains: O, R
Molecule details ›
Chains: O, R
Length: 56 amino acids
Theoretical weight: 6.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P02676 (Residues: 61-116; Coverage: 12%)
Gene name: FGB
Sequence domains: Fibrinogen alpha/beta chain family
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Fibrinogen gamma-B chain Chains: P, S
Molecule details ›
Chains: P, S
Length: 48 amino acids
Theoretical weight: 5.48 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P12799 (Residues: 25-72; Coverage: 11%)
Gene name: FGG
Sequence domains: Fibrinogen alpha/beta chain family
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P212121
Unit cell:
a: 53.7Å b: 59.1Å c: 97.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.22

Quick links

Citations

12 review citations

The molecular basis of quantitative fibrinogen disorders.
Asselta et al. (2006)
11 more

1 mention without citation

Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution.
Madrazo et al. (2001)