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Structure paper

TitleActivity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei.
Journal, issue, pagesJ. Mol. Biol., Vol. 264, Page 337-349, Year 1996
Publish dateAug 24, 1996 (structure data deposition date)
AuthorsStahlberg, J. / Divne, C. / Koivula, A. / Piens, K. / Claeyssens, M. / Teeri, T.T. / Jones, T.A.
External linksJ. Mol. Biol. / PubMed:8951380
MethodsX-ray diffraction
Resolution2 - 2.2 Å
Structure data

PDB-2cel:
ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3cel:
ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH CELLOBIOSE BOUND IN THE ACTIVE SITE
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4cel:
ACTIVE-SITE MUTANT D214N DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CD:
Unknown entry

Source
  • hypocrea jecorina (fungus)
KeywordsHYDROLASE / CELLULOSE DEGRADATION / GLYCOSIDASE / GLYCOPROTEIN

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