› 1rf0

X-ray diffraction
2.81Å resolution

Crystal Structure of Fragment D of gammaE132A Fibrinogen

Released:
DOI: 10.2210/pdb1rf0/pdb
PDB entry 1rf0 coloured by chain, front view.
PDB entry 1rf0 coloured by chain, side view.
PDB entry 1rf0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Calcium-binding site beta 2, adjacent to the "b" polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization.
Kostelansky MS, Lounes KC, Ping LF, Dickerson SK, Gorkun OV, Lord ST
Biochemistry 43 2475-83 (2004)
PMID: 14992585

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-136001 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Fibrinogen alpha chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 66 amino acids
Theoretical weight: 7.75 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P02671 (Residues: 145-210; Coverage: 8%)
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: B, E
Molecule details ›
Chains: B, E
Length: 313 amino acids
Theoretical weight: 35.94 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P02675 (Residues: 179-491; Coverage: 68%)
Gene name: FGB
Sequence domains:
Structure domains:
Fibrinogen gamma chain Chains: C, F
Molecule details ›
Chains: C, F
Length: 311 amino acids
Theoretical weight: 35.16 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P02679 (Residues: 122-432; Coverage: 73%)
Gene names: FGG, PRO2061
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NAG 2 x NAG
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 88.408Å b: 94.948Å c: 227.614Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.286
Expression system: Cricetulus griseus

Quick links

Citations

4 review citations

Mechanisms of fibrin polymerization and clinical implications.
Weisel et al. (2013)
3 more

2 mentions without citation

Impaired protofibril formation in fibrinogen gamma N308K is due to altered D:D and "A:a" interactions.
Bowley et al. (2009)
1 more