› 1a2c

X-ray diffraction
2.1Å resolution

Structure of thrombin inhibited by AERUGINOSIN298-A from a BLUE-GREEN ALGA

Released:
DOI: 10.2210/pdb1a2c/pdb
PDB entry 1a2c coloured by chain, front view.
PDB entry 1a2c coloured by chain, side view.
PDB entry 1a2c coloured by chain, top view.
Source organisms:
Primary publication:
Structure of Thrombin Inhibited by Aeruginosin 298-A from a Blue-Green Alga
Steiner JLR, Murakami M, Tulinsky A
J. Am. Chem. Soc. 120 597- (1998)

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133077 (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
UniProt:
  • Canonical: P00734 (Residues: 328-363; Coverage: 6%)
Gene name: F2
Sequence domains: Thrombin light chain
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
Hirudin variant-2 Chain: I
Molecule details ›
Chain: I
Length: 12 amino acids
Theoretical weight: 1.53 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
  • Canonical: P09945 (Residues: 60-71; Coverage: 19%)
Aeruginosin 298-A Chain: J
Molecule details ›
Chain: J
Length: 4 amino acids
Theoretical weight: 605 Da
Source organism: Microcystis aeruginosa

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
2 modified residues:
Ligand TYS 1 x TYS
Ligand PRJ 1 x PRJ

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 71.97Å b: 72.48Å c: 72.24Å
α: 90° β: 100.93° γ: 90°
R-values:
R R work R free
0.15 0.15 not available
Expression system: Not provided

Quick links

Citations

1 mention without citation

Deciphering Key Pharmacological Pathways of Qingdai Acting on Chronic Myeloid Leukemia Using a Network Pharmacology-Based Strategy.
Li et al. (2018)