1g5t

X-ray diffraction
1.8Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF ATP:CORRINOID ADENOSYLTRANSFERASE FROM SALMONELLA TYPHIMURIUM. APO-ATP FORM

Released:

Function and Biology Details

Reaction catalysed:
(1a) 2 cob(II)alamin + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)alamin
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Corrinoid adenosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 21.75 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Salmonella enterica subsp. enterica serovar Typhimurium
UniProt:
  • Canonical: P31570 (Residues: 1-196; Coverage: 100%)
Gene names: STM1718, btuR, cobA
Sequence domains: ATP:corrinoid adenosyltransferase BtuR/CobO/CobP
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6522
Unit cell:
a: 49.5Å b: 49.5Å c: 249.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.192 0.267
Expression system: Salmonella enterica subsp. enterica serovar Typhimurium