› 4knv

X-ray diffraction
1.99Å resolution

Function and Biology Details

Reaction catalysed: 
N-acylneuraminate 9-phosphate + H(2)O = N-acylneuraminate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acylneuraminate-9-phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 27.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8TBE9 (Residues: 7-242; Coverage: 95%)
Gene names: C20orf147, HDHD4, NANP
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PO4 2 x PO4
Ligand MG 2 x MG
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P1
Unit cell:
a: 46.34Å b: 53.436Å c: 63.958Å
α: 65.5° β: 74.99° γ: 85.17°
R-values:
R R work R free
0.201 0.2 0.246
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Designing sugar mimetics: non-natural pyranosides as innovative chemical tools.
Saliba et al. (2016)
1 other article

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)