› 1fzg

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE

Released:
DOI: 10.2210/pdb1fzg/pdb
PDB entry 1fzg coloured by chain, front view.
PDB entry 1fzg coloured by chain, side view.
PDB entry 1fzg 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

Assembly composition:
hetero decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136021 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (5 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:
Fibrinogen beta chain Chains: M, N, S, T
Molecule details ›
Chains: M, N, S, T
Length: 4 amino acids
Theoretical weight: 468 Da
Source organism: Homo sapiens
UniProt:
  • Canonical: P02675 (Residues: 45-48; Coverage: 1%)
Gene name: FGB

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand CA 8 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 54.8Å b: 149.4Å c: 234.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.302

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

5 mentions without citation

Biochemical and structural analysis of the interaction between β-amyloid and fibrinogen.
Zamolodchikov et al. (2016)
4 more