PDBe 2a45

X-ray diffraction
3.65Å resolution

Crystal structure of the complex between thrombin and the central "E" region of fibrin

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero decamer (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):
Thrombin light chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 328-363; Coverage: 6%)
Gene name: F2
Thrombin heavy chain Chains: B, E
Molecule details ›
Chains: B, E
Length: 259 amino acids
Theoretical weight: 29.78 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Fibrinogen alpha chain Chains: G, J
Molecule details ›
Chains: G, J
Length: 57 amino acids
Theoretical weight: 6.64 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02671 (Residues: 36-92; Coverage: 7%)
Gene name: FGA
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Fibrinogen beta chain Chains: H, K
Molecule details ›
Chains: H, K
Length: 91 amino acids
Theoretical weight: 9.79 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02675 (Residues: 45-135; Coverage: 20%)
Gene name: FGB
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Fibrinogen gamma chain Chains: I, L
Molecule details ›
Chains: I, L
Length: 45 amino acids
Theoretical weight: 5.1 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02679 (Residues: 27-71; Coverage: 11%)
Gene names: FGG, PRO2061
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P31
Unit cell:
a: 76.263Å b: 76.263Å c: 192.452Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 not available 0.29