› 1fze

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN

Released:
DOI: 10.2210/pdb1fze/pdb
PDB entry 1fze coloured by chain, front view.
PDB entry 1fze coloured by chain, side view.
PDB entry 1fze coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide.
Everse SJ, Spraggon G, Veerapandian L, Doolittle RF
Biochemistry 38 2941-6 (1999)
PMID: 10074346

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero hexamer
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: 87 amino acids
Theoretical weight: 10.24 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02671 (Residues: 130-216; Coverage: 10%)
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: 328 amino acids
Theoretical weight: 37.69 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02675 (Residues: 164-491; Coverage: 71%)
Gene name: FGB
Sequence domains:
Structure domains:
Fibrinogen gamma chain Chains: C, F
Molecule details ›
Chains: C, F
Length: 319 amino acids
Theoretical weight: 36.22 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02679 (Residues: 114-432; Coverage: 75%)
Gene names: FGG, PRO2061
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NAG 4 x NAG
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21
Unit cell:
a: 108Å b: 48.6Å c: 166.4Å
α: 90° β: 104.4° γ: 90°
R-values:
R R work R free
0.251 0.251 0.318

Quick links

Citations

7 review citations

A comparison of the mechanical and structural properties of fibrin fibers with other protein fibers.
Guthold et al. (2007)
6 more

1 mention without citation

A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptides.
Yang et al. (2000)