X-ray diffraction
3.6Å resolution

Crystal structure of D-dimer from human fibrin complexed with Gly-His-Arg-Pro-Tyr-amide


Function and Biology Details

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (5 distinct):
Fibrinogen alpha chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 197 amino acids
Theoretical weight: 22.77 KDa
Source organism: Homo sapiens
  • Canonical: P02671 (Residues: 20-216; Coverage: 23%)
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
Fibrinogen gamma chain Chains: C, F
Molecule details ›
Chains: C, F
Length: 317 amino acids
Theoretical weight: 35.82 KDa
Source organism: Homo sapiens
  • Canonical: P02679 (Residues: 121-433; Coverage: 73%)
  • Best match: P02679-2 (Residues: 121-437)
Gene names: FGG, PRO2061
Sequence domains: Fibrinogen beta and gamma chains, C-terminal globular domain
Structure domains:
Fibrinogen beta chain Chains: M, N
Molecule details ›
Chains: M, N
Length: 5 amino acids
Theoretical weight: 631 Da
Source organism: Bos taurus
Expression system: Not provided
  • Canonical: P02676 (Residues: 22-26; Coverage: 1%)
Gene name: FGB

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, MAN, GAL, SIA
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: C2
Unit cell:
a: 264.72Å b: 97.32Å c: 132.49Å
α: 90° β: 122.78° γ: 90°
R R work R free
0.263 0.263 0.32
Expression system: Not provided