2qq2

X-ray diffraction
2.8Å resolution

Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7

Released:
Source organism: Homo sapiens
Entry authors: Busam R, Lehtio L, Arrowsmith CH, Berglund H, Collins R, Dahlgren LG, Herman MD, Edwards A, Flodin S, Flores A, Graslund S, Hammarstrom M, Hallberg BM, Holmberg-Schiavone L, Johansson I, Kallas A, Karlberg T, Kotenyova T, Moche M, Nordlund P, Nyman T, Sagemark J, Stenmark P, Sundstrom M, Thorsell AG, Tresaugues L, van den Berg S, Weigelt J, Welin M, Persson C, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
Palmitoyl-CoA + H(2)O = CoA + palmitate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosolic acyl coenzyme A thioester hydrolase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 193 amino acids
Theoretical weight: 21.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O00154 (Residues: 209-378; Coverage: 45%)
Gene names: ACOT7, BACH
Sequence domains: Thioesterase superfamily
Structure domains: Hotdog Thioesterase

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P1
Unit cell:
a: 80.95Å b: 81.6Å c: 105.1Å
α: 79.61° β: 89.7° γ: 74.12°
R-values:
R R work R free
0.217 0.216 0.239
Expression system: Escherichia coli BL21(DE3)