› 6e8l

X-ray diffraction
2.3Å resolution

Crystal Structure of Alkyl hydroperoxidase D (AhpD) from Streptococcus pneumoniae (Strain D39/ NCTC 7466)

Released:
DOI: 10.2210/pdb6e8l/pdb
PDB entry 6e8l coloured by chain, front view.
PDB entry 6e8l coloured by chain, side view.
PDB entry 6e8l coloured by chain, top view.
Source organism: Streptococcus pneumoniae D39
Primary publication:
Structure-function analyses of alkylhydroperoxidase D from Streptococcus pneumoniae reveal an unusual three-cysteine active site architecture.
Meng Y, Sheen CR, Magon NJ, Hampton MB, Dobson RCJ
J Biol Chem 295 2984-2999 (2020)
PMID: 31974167

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxymuconolactone decarboxylase-like domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 183 amino acids
Theoretical weight: 19.85 KDa
Source organism: Streptococcus pneumoniae D39
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2ZNM1 (Residues: 2-182; Coverage: 100%)
Gene name: SPD_0373
Sequence domains: Carboxymuconolactone decarboxylase family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 65.296Å b: 84.233Å c: 183.846Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

ClpX/P-Dependent Degradation of Novel Substrates in Streptococcus mutans.
Gurung et al. (2022)
2 more

1 mention without citation

Structure-function analyses of alkylhydroperoxidase D from Streptococcus pneumoniae reveal an unusual three-cysteine active site architecture.
Meng et al. (2020)