Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero decamer (preferred)
Assembly name:
Fibrin complex and peptide (preferred)
PDBe Complex ID:
PDB-CPX-215133 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (8 distinct):
Fibrinogen alpha chain
Molecule details ›
Chains: A, D, G, J
Length: 562 amino acids
Theoretical weight: 60.97 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 562 amino acids
Theoretical weight: 60.97 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P02671 (Residues: 20-581; Coverage: 66%)
Sequence domains:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Fibrinogen beta chain
Molecule details ›
Chains: B, E, H, K
Length: 461 amino acids
Theoretical weight: 52.38 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains:
Structure domains:
Length: 461 amino acids
Theoretical weight: 52.38 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P02675 (Residues: 31-491; Coverage: 100%)
Sequence domains:
Structure domains:
Fibrinogen gamma chain
Molecule details ›
Chains: C, F, I, L
Length: 411 amino acids
Theoretical weight: 46.52 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains:
Structure domains:
Length: 411 amino acids
Theoretical weight: 46.52 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P02679 (Residues: 27-433; Coverage: 95%)
Sequence domains:
Structure domains:
Ligands and Environments
1 bound ligand:
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 8.2.2
Spacegroup:
P21
