› 2a8i

X-ray diffraction
2Å resolution

Crystal Structure of human Taspase1

Released:
DOI: 10.2210/pdb2a8i/pdb
PDB entry 2a8i coloured by chain, front view.
PDB entry 2a8i coloured by chain, side view.
PDB entry 2a8i 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: 44.84 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q9H6P5 (Residues: 1-420; Coverage: 100%)
Gene names: C20orf13, TASP1
Sequence domains: Asparaginase

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2221
Unit cell:
a: 124.782Å b: 126.068Å c: 117.923Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.26

Quick links

Citations

3 review citations

Cleaving for growth: threonine aspartase 1--a protease relevant for development and disease.
Stauber et al. (2016)
2 more

5 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
4 more