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Structure paper

TitleStructural Studies of a Thermophilic Esterase from a New Planctomycetes Species, Thermogutta Terrifontis.
Journal, issue, pagesFEBS J., Vol. 282, Page 2846-, Year 2015
Publish dateMar 24, 2015 (structure data deposition date)
AuthorsSayer, C. / Isupov, M.N. / Bonch-Osmolovskaya, E. / Littlechild, J.A.
External linksFEBS J. / PubMed:26011036
MethodsX-ray diffraction
Resolution1.03 - 1.16 Å
Structure data

PDB-4uhc:
Structural studies of a thermophilic esterase from Thermogutta terrifontis (Native)
Method: X-RAY DIFFRACTION / Resolution: 1.03 Å

PDB-4uhd:
Structural studies of a thermophilic esterase from Thermogutta terrifontis (acetate bound)
Method: X-RAY DIFFRACTION / Resolution: 1.07 Å

PDB-4uhe:
Structural studies of a thermophilic esterase from Thermogutta terrifontis (malate bound)
Method: X-RAY DIFFRACTION / Resolution: 1.16 Å

PDB-4uhf:
Structural studies of a thermophilic esterase from Thermogutta terrifontis (L37A mutant with butyrate bound)
Method: X-RAY DIFFRACTION / Resolution: 1.08 Å

PDB-4uhh:
Structural studies of a thermophilic esterase from Thermogutta terrifontis (cacodylate complex)
Method: X-RAY DIFFRACTION / Resolution: 1.06 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-MLT:
D-MALATE

ChemComp-CAD:
CACODYLIC ACID

ChemComp-BUA:
butanoic acid

Source
  • planctomycetes bacterium r1 (bacteria)
KeywordsHYDROLASE / ALPHA BETA HYDROLASE

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