› 6xml

X-ray diffraction
1.88Å resolution

Human aldolase A I98C

Released:
DOI: 10.2210/pdb6xml/pdb
PDB entry 6xml coloured by chain, front view.
PDB entry 6xml coloured by chain, side view.
PDB entry 6xml coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Substitutions at a rheostat position in human aldolase A cause a shift in the conformational population.
Fenton KD, Meneely KM, Wu T, Martin TA, Swint-Kruse L, Fenton AW, Lamb AL
Protein Sci 31 357-370 (2022)
PMID: 34734672

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 364 amino acids
Theoretical weight: 39.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04075 (Residues: 1-364; Coverage: 100%)
Gene names: ALDA, ALDOA
Sequence domains: Fructose-bisphosphate aldolase class-I

Ligands and Environments

2 bound ligands:
Ligand PO4 4 x PO4
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P6422
Unit cell:
a: 162.571Å b: 162.571Å c: 167.797Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.245 0.286
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Structural Plasticity Is a Feature of Rheostat Positions in the Human Na+/Taurocholate Cotransporting Polypeptide (NTCP).
Ruggiero et al. (2022)
2 more

2 mentions without citation

Substitutions at a rheostat position in human aldolase A cause a shift in the conformational population.
Fenton et al. (2022)
1 more