› 1re3

X-ray diffraction
2.45Å resolution

Crystal Structure of Fragment D of BbetaD398A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide

Released:
DOI: 10.2210/pdb1re3/pdb
PDB entry 1re3 coloured by chain, front view.
PDB entry 1re3 coloured by chain, side view.
PDB entry 1re3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
B beta Glu397 and B beta Asp398 but not B beta Asp432 are required for "B:b" interactions.
Kostelansky MS, Bolliger-Stucki B, Betts L, Gorkun OV, Lord ST
Biochemistry 43 2465-74 (2004)
PMID: 14992584

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-136003 (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: 35.9 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: 35.22 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:
GHRP peptide Chains: G, H
Molecule details ›
Chains: G, H
Length: 4 amino acids
Theoretical weight: 468 Da

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand CA 5 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 54.514Å b: 147.665Å c: 229.716Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 0.263
Expression system: Cricetulus griseus

Quick links

Citations

7 citation in other articles

Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions.
Litvinov et al. (2007)
6 more

4 mentions without citation

Structural genomics reveals EVE as a new ASCH/PUA-related domain.
Bertonati et al. (2009)
3 more