› 4ygq

X-ray diffraction
2Å resolution

Crystal structure of HAD phosphatase from Thermococcus onnurineus

Released:
DOI: 10.2210/pdb4ygq/pdb
PDB entry 4ygq coloured by chain, front view.
PDB entry 4ygq coloured by chain, side view.
PDB entry 4ygq coloured by chain, top view.
Source organism: Thermococcus onnurineus NA1
Primary publication:
Structural basis for the substrate selectivity of a HAD phosphatase from Thermococcus onnurineus NA1.
Ngo TD, Van Le B, Subramani VK, Thi Nguyen CM, Lee HS, Cho Y, Kim KK, Hwang HY
Biochem Biophys Res Commun 461 122-7 (2015)
PMID: 25858319

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110408 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde 3-phosphate phosphatase Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 26.76 KDa
Source organism: Thermococcus onnurineus NA1
Expression system: Escherichia coli
UniProt:
  • Canonical: B6YTD6 (Residues: 1-214; Coverage: 100%)
Gene name: TON_0338
Sequence domains: haloacid dehalogenase-like hydrolase

Ligands and Environments

1 bound ligand:
Ligand TBU 1 x TBU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: C2
Unit cell:
a: 121.193Å b: 62.991Å c: 37.541Å
α: 90° β: 106.5° γ: 90°
R-values:
R R work R free
0.168 0.166 0.202
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Engineering substrate specificity of HAD phosphatases and multienzyme systems development for the thermodynamic-driven manufacturing sugars.
Tian et al. (2022)
1 more