› 4kxx

X-ray diffraction
1.03Å resolution

Human transketolase in covalent complex with donor ketose D-sedoheptulose-7-phosphate

Released:
DOI: 10.2210/pdb4kxx/pdb
PDB entry 4kxx coloured by chain, front view.
PDB entry 4kxx coloured by chain, side view.
PDB entry 4kxx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Sub-ångström-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediate.
Lüdtke S, Neumann P, Erixon KM, Leeper F, Kluger R, Ficner R, Tittmann K
Nat Chem 5 762-7 (2013)
PMID: 23965678

Function and Biology Details

Reaction catalysed: 
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151464 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transketolase Chain: A
Molecule details ›
Chain: A
Length: 637 amino acids
Theoretical weight: 69.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P29401 (Residues: 1-623; Coverage: 100%)
Gene name: TKT
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 1 x TPP
4 bound ligands:
Ligand 1Y7 1 x 1Y7
Ligand EDO 12 x EDO
Ligand MG 1 x MG
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 113.675Å b: 86.097Å c: 73.017Å
α: 90° β: 125.43° γ: 90°
R-values:
R R work R free
0.119 0.117 0.148
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Transition metal catalysis in confined spaces.
Leenders et al. (2015)
4 more

1 mention without citation

QM/MM Study of Human Transketolase: Thiamine Diphosphate Activation Mechanism and Complete Catalytic Cycle.
Nauton et al. (2021)