› 6no0

X-ray diffraction
2.21Å resolution

ADP bound to ATP-grasp fold of Blastocystis hominis succinyl-CoA synthetase

Released:
DOI: 10.2210/pdb6no0/pdb
PDB entry 6no0 coloured by chain, front view.
PDB entry 6no0 coloured by chain, side view.
PDB entry 6no0 coloured by chain, top view.
Source organism: Blastocystis sp. ATCC 50177/Nand II
Primary publication:
ATP-specificity of succinyl-CoA synthetase from Blastocystis hominis.
Huang J, Nguyen VH, Hamblin KA, Maytum R, van der Giezen M, Fraser ME
Acta Crystallogr D Struct Biol 75 647-659 (2019)
PMID: 31282474

Function and Biology Details

Reaction catalysed: 
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109843 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Succinate--CoA ligase [ADP-forming] subunit beta Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 27.61 KDa
Source organism: Blastocystis sp. ATCC 50177/Nand II
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B3FHP0 (Residues: 15-253; Coverage: 58%)
Gene name: SCSb
Sequence domains: ATP-grasp domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2221
Unit cell:
a: 92.203Å b: 116.981Å c: 127.161Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.213 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Second distinct conformation of the phosphohistidine loop in succinyl-CoA synthetase.
Huang et al. (2021)
1 more