› 3hus

X-ray diffraction
3.04Å resolution

Crystal structure of recombinant gamma N308K fibrinogen fragment D with the peptide ligand Gly-Pro-Arg-Pro-amide

Released:
DOI: 10.2210/pdb3hus/pdb
PDB entry 3hus coloured by chain, front view.
PDB entry 3hus coloured by chain, side view.
PDB entry 3hus coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Impaired protofibril formation in fibrinogen gamma N308K is due to altered D:D and "A:a" interactions.
Bowley SR, Okumura N, Lord ST
Biochemistry 48 8656-63 (2009)
PMID: 19650644

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
PDBe Complex ID:
PDB-CPX-136015 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (5 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: 35.23 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:
Peptide Ligand Gly-Pro-Arg-Pro-amide Chains: G, H, I, J
Molecule details ›
Chains: G, H, I, J
Length: 4 amino acids
Theoretical weight: 426 Da

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P43212
Unit cell:
a: 95.009Å b: 95.009Å c: 448.382Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.22 0.288
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