› 7nnk

X-ray diffraction
1.8Å resolution

Crystal structure of S116A mutant of hydroxy ketone aldolase (SwHKA) from Sphingomonas wittichii RW1 in complex with hydroxypyruvate

Released:
DOI: 10.2210/pdb7nnk/pdb
Model geometry
Fit model/data
PDB entry 7nnk coloured by chain, front view.
PDB entry 7nnk coloured by chain, side view.
PDB entry 7nnk coloured by chain, top view.
Source organism: Rhizorhabdus wittichii RW1
Primary publication:
Substrate Induced Movement of the Metal Cofactor between Active and Resting State.
Marsden SR, Wijma HJ, Mohr MKF, Justo I, Hagedoorn PL, Laustsen J, Jeffries CM, Svergun D, Mestrom L, McMillan DGG, Bento I, Hanefeld U
OpenAccess logo Angew Chem Int Ed Engl (2022)
PMID: 36214476

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-303652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HpcH/HpaI aldolase/citrate lyase domain-containing protein; Hydroxypyruvate/pyruvate aldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 26.77 KDa
Source organism: Rhizorhabdus wittichii RW1
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A9J9HGY6 (Residues: 2-115; Coverage: 45%)
  • Canonical: A0AAT8XT72 (Residues: 117-252; Coverage: 54%)
Gene name: Swit_5035
Sequence domains: HpcH/HpaI aldolase/citrate lyase

Ligands and Environments

2 bound ligands:
Ligand 3PY 1 x 3PY
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: R3
Unit cell:
a: 71.327Å b: 71.327Å c: 223.185Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.183 0.225
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Substrate Induced Movement of the Metal Cofactor between Active and Resting State.
Marsden et al. (2022)