1qno: Difference between revisions
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|PDB= 1qno |SIZE=350|CAPTION= <scene name='initialview01'>1qno</scene>, resolution 2.00Å | |PDB= 1qno |SIZE=350|CAPTION= <scene name='initialview01'>1qno</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=MAN:Mannan+Binding+Site'>MAN</scene> | |SITE= <scene name='pdbsite=MAN:Mannan+Binding+Site'>MAN</scene> | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qno OCA], [http://www.ebi.ac.uk/pdbsum/1qno PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qno RCSB]</span> | |||
}} | }} | ||
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[[Category: Siika-Aho, M.]] | [[Category: Siika-Aho, M.]] | ||
[[Category: Wilson, K S.]] | [[Category: Wilson, K S.]] | ||
[[Category: anomalous scattering]] | [[Category: anomalous scattering]] | ||
[[Category: mannanase]] | [[Category: mannanase]] | ||
[[Category: trichoderma reesei]] | [[Category: trichoderma reesei]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:16:23 2008'' | ||
Revision as of 23:16, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Mannan endo-1,4-beta-mannosidase, with EC number 3.2.1.78 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE 3-D STRUCTURE OF A TRICHODERMA REESEI B-MANNANASE FROM GLYCOSIDE HYDROLASE FAMILY 5
OverviewOverview
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.
About this StructureAbout this Structure
1QNO is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of a Trichoderma reesei beta-mannanase from glycoside hydrolase family 5., Sabini E, Schubert H, Murshudov G, Wilson KS, Siika-Aho M, Penttila M, Acta Crystallogr D Biol Crystallogr. 2000 Jan;56(Pt 1):3-13. PMID:10666621
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