› 4umd

X-ray diffraction
2.29Å resolution

Crystal structure of 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Moraxella catarrhalis in complex with citrate

Released:
DOI: 10.2210/pdb4umd/pdb
Model geometry
Fit model/data
PDB entry 4umd coloured by chain, front view.
PDB entry 4umd coloured by chain, side view.
PDB entry 4umd coloured by chain, top view.
Source organism: Moraxella catarrhalis BC8
Primary publication:
Ligand-bound structures of 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Moraxella catarrhalis reveal a water channel connecting to the active site for the second step of catalysis.
Dhindwal S, Priyadarshini P, Patil DN, Tapas S, Kumar P, Tomar S, Kumar P
Acta Crystallogr D Biol Crystallogr 71 239-55 (2015)
PMID: 25664734

Function and Biology Details

Reaction catalysed: 
3-deoxy-D-manno-octulosonate 8-phosphate + H(2)O = 3-deoxy-D-manno-octulosonate + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102258 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC Chain: A
Molecule details ›
Chain: A
Length: 193 amino acids
Theoretical weight: 21.08 KDa
Source organism: Moraxella catarrhalis BC8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0J9X241 (Residues: 1-173; Coverage: 100%)
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains: HAD superfamily/HAD-like

Ligands and Environments

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

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BRUKER AXS MICROSTAR-H
Spacegroup: I4
Unit cell:
a: 86.394Å b: 86.394Å c: 40.802Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.176 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Structural and thermodynamic characterization of metal binding in Vps29 from Entamoeba histolytica: implication in retromer function.
Srivastava et al. (2017)