› 2a8m

X-ray diffraction
2.6Å resolution

Crystal Structure of Human Taspase1 (T234S mutant)

Released:
DOI: 10.2210/pdb2a8m/pdb
PDB entry 2a8m coloured by chain, front view.
PDB entry 2a8m coloured by chain, side view.
PDB entry 2a8m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human Taspase1, a crucial protease regulating the function of MLL.
Khan JA, Dunn BM, Tong L
Structure 13 1443-52 (2005)
PMID: 16216576

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190639 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine aspartase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 420 amino acids
Theoretical weight: 44.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H6P5 (Residues: 1-420; Coverage: 100%)
Gene names: C20orf13, TASP1
Sequence domains: Asparaginase

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 60.441Å b: 89.371Å c: 104.276Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.29
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Taspase1: a 'misunderstood' protease with translational cancer relevance.
Wünsch et al. (2016)
2 more

1 mention without citation

Unraveling the Activation Mechanism of Taspase1 which Controls the Oncogenic AF4-MLL Fusion Protein.
Sabiani et al. (2015)