› 2fea

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-en-1-yl phosphate + H(2)O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 236 amino acids
Theoretical weight: 27.42 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O31667 (Residues: 1-235; Coverage: 100%)
Gene names: BSU13600, mtnX, ykrX
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand ZN 2 x ZN
Ligand EDO 10 x EDO
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 59.013Å b: 43.104Å c: 109.553Å
α: 90° β: 98.91° γ: 90°
R-values:
R R work R free
0.163 0.16 0.217
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

MtnBD is a multifunctional fusion enzyme in the methionine salvage pathway of Tetrahymena thermophila.
Nakano et al. (2013)

6 mentions without citation

Small-molecule MDM2/X inhibitors and PROTAC degraders for cancer therapy: advances and perspectives.
Fang et al. (2020)
5 more