› 1fid

X-ray diffraction
2.1Å resolution

STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT

Released:
DOI: 10.2210/pdb1fid/pdb
PDB 1fid coloured by chain and viewed from the front.
PDB 1fid coloured by chain and viewed from the side.
PDB 1fid coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen.
Yee VC, Pratt KP, Côté HC, Trong IL, Chung DW, Davie EW, Stenkamp RE, Teller DC
Structure 5 125-38 (1997)
PMID: 9016719

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibrinogen gamma chain Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 30.24 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P02679 (Residues: 169-433; Coverage: 62%)
  • Best match: P02679-2 (Residues: 169-437)
Gene names: FGG, PRO2061
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 84.36Å b: 62.56Å c: 49.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 0.226
Expression system: Komagataella pastoris

Quick links

Citations

17 review citations

Fibrin Formation, Structure and Properties.
Weisel et al. (2017)
16 more

3 mentions without citation

Fibrinogen-Related Proteins in Tissue Repair: How a Unique Domain with a Common Structure Controls Diverse Aspects of Wound Healing.
Zuliani-Alvarez et al. (2015)
2 more