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TitleStructure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus.
Journal, issue, pagesProteins, Vol. 82, Page 3217-3223, Year 2014
Publish dateFeb 4, 2014 (structure data deposition date)
AuthorsKim, M.K. / An, Y.J. / Song, J.M. / Jeong, C.S. / Kang, M.H. / Kwon, K.K. / Lee, Y.H. / Cha, S.S.
External linksProteins / PubMed:25082572
MethodsX-ray diffraction
Resolution2.36 - 2.6 Å
Structure data

PDB-4oou:
Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

PDB-4ooz:
Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus in complex with mannopentaose
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-BMA:
beta-D-mannopyranose

Source
  • cryptopygus antarcticus (arthropod)
KeywordsHYDROLASE / Tim Barrel

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