PDBe 1tmt

X-ray diffraction
2.2Å resolution

CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Thrombin light chain Chain: L
Molecule details ›
Chain: L
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00734 (Residues: 328-363; Coverage: 6%)
Gene name: F2
Thrombin heavy chain Chain: H
Molecule details ›
Chain: H
Length: 259 amino acids
Theoretical weight: 29.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Hirudin variant-1 Chain: I
Molecule details ›
Chain: I
Length: 3 amino acids
Theoretical weight: 419 Da
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
  • Canonical: P01050 (Residues: 46-47; Coverage: 3%)
Hirudin-2 Chain: J
Molecule details ›
Chain: J
Length: 18 amino acids
Theoretical weight: 1.91 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
  • Canonical: P28504 (Residues: 53-65; Coverage: 20%)

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 80.5Å b: 107.1Å c: 45.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 not available
Expression systems:
  • Escherichia coli
  • Not provided