5e8e

X-ray diffraction
1.9Å resolution

Crystal structure of thrombin bound to an exosite 1-specific IgA Fab

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-208302 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (6 distinct):
IGA FAB LIGHT CHAIN Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 23.54 KDa
Source organism: Homo sapiens
Structure domains: Immunoglobulins
IGA FAB HEAVY CHAIN Chain: B
Molecule details ›
Chain: B
Length: 229 amino acids
Theoretical weight: 24.77 KDa
Source organism: Homo sapiens
Structure domains: Immunoglobulins
Thrombin heavy chain Chain: H
Molecule details ›
Chain: H
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
Thrombin light chain Chain: L
Molecule details ›
Chain: L
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 328-363; Coverage: 6%)
Gene name: F2
Sequence domains: Thrombin light chain

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, GAL, SIA
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 66.769Å b: 92.229Å c: 147.487Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.201 0.244