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1QNQ

The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5

Summary for 1QNQ
Entry DOI10.2210/pdb1qnq/pdb
Related1QNO 1QNP 1QNR 1QNS
DescriptorENDO-1,4-B-D-MANNANASE, 2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride, SULFATE ION, ... (5 entities in total)
Functional Keywordshydrolase, mannanase, trichoderma reesei, anomalous scattering
Biological sourceTRICHODERMA REESEI
Total number of polymer chains1
Total formula weight39751.69
Authors
Sabini, E.,Schubert, H.,Murshudov, G.,Wilson, K.S.,Siika-Aho, M.,Penttila, M. (deposition date: 1999-10-20, release date: 2000-10-19, Last modification date: 2024-11-13)
Primary citationSabini, E.,Schubert, H.,Murshudov, G.,Wilson, K.S.,Siika-Aho, M.,Penttila, M.
The Three-Dimensional Structure of a Trichoderma Reesei Beta-Mannanase from Glycoside Hydrolase Family 5.
Acta Crystallogr.,Sect.D, 56:3-, 2000
Cited by
PubMed Abstract: The crystal structure of the catalytic core domain of beta-mannanase from the fungus Trichoderma reesei has been determined at a resolution of 1.5 A. The structure was solved using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P2(1). The map computed with the experimental phases was enhanced by the application of an automated model building and refinement procedure using the amplitudes and experimental phases as observations. This approach is expected to be of more general application. The structure of the native enzyme and complexes with Tris-HCl and mannobiose are also reported: the mannobiose binds in subsites +1 and +2. The structure is briefly compared with that of the homologous beta-mannanase from the bacterium Thermomonospora fusca.
PubMed: 10666621
DOI: 10.1107/S0907444999013943
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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