› 8q5a

X-ray diffraction
2.8Å resolution

Crystal structure of metal-dependent class II sulfofructosephosphate aldolase from Hafnia paralvei HpSqiA-Zn in complex with dihydroxyacetone phosphate (DHAP)

Released:
DOI: 10.2210/pdb8q5a/pdb
Model geometry
Fit model/data
PDB entry 8q5a coloured by chain, front view.
PDB entry 8q5a coloured by chain, side view.
PDB entry 8q5a coloured by chain, top view.
Source organism: Hafnia paralvei
Primary publication:
Defining the molecular architecture, metal dependence, and distribution of metal-dependent class II sulfofructose-1-phosphate aldolases.
Sharma M, Kaur A, Soler NM, Lingford JP, Epa R, Goddard-Borger ED, Davies GJ, Williams SJ
OpenAccess logo J Biol Chem 105338 (2023)
PMID: 37838169

Function and Biology Details

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-233083 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ketose-bisphosphate aldolase Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 33.59 KDa
Source organism: Hafnia paralvei
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A2A2MA06 (Residues: 1-287; Coverage: 100%)
Gene names: CJD50_15755, agaY, kbaY
Sequence domains: Fructose-bisphosphate aldolase class-II

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand 13P 1 x 13P
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: I222
Unit cell:
a: 64.605Å b: 87.669Å c: 103.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.274
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Defining the molecular architecture, metal dependence, and distribution of metal-dependent class II sulfofructose-1-phosphate aldolases.
Sharma et al. (2023)