PDBe 1m3u

X-ray diffraction
1.8Å resolution

Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate

Released:

Function and Biology Details

Reaction catalysed:
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-methyl-2-oxobutanoate hydroxymethyltransferase Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 264 amino acids
Theoretical weight: 28.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P31057 (Residues: 1-264; Coverage: 100%)
Gene names: JW0130, b0134, panB
Sequence domains: Ketopantoate hydroxymethyltransferase
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 86.074Å b: 157.17Å c: 100.181Å
α: 90° β: 97.44° γ: 90°
R-values:
R R work R free
0.158 0.152 0.193
Expression system: Escherichia coli