1gbg: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1gbg |SIZE=350|CAPTION= <scene name='initialview01'>1gbg</scene>, resolution 1.8Å | |PDB= 1gbg |SIZE=350|CAPTION= <scene name='initialview01'>1gbg</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbg OCA], [http://www.ebi.ac.uk/pdbsum/1gbg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gbg RCSB]</span> | |||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Hahn, M.]] | [[Category: Hahn, M.]] | ||
[[Category: Heinemann, U.]] | [[Category: Heinemann, U.]] | ||
[[Category: hydrolase (glucanase)]] | [[Category: hydrolase (glucanase)]] | ||
''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 20:40:40 2008'' | ||
Revision as of 17:40, 30 March 2008
| |||||||||||||
| 1gbg, resolution 1.8Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | CA | ||||||||||||
| Activity: | Licheninase, with EC number 3.2.1.73 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
BACILLUS LICHENIFORMIS BETA-GLUCANASE
Overview
The crystal structure of the 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 A and refined to R = 16.5%. The protein has a similar beta-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-beta-D-glucan 4-glucanohydrolases.
About this Structure
1GBG is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.
Reference
Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution., Hahn M, Pons J, Planas A, Querol E, Heinemann U, FEBS Lett. 1995 Oct 30;374(2):221-4. PMID:7589539
Page seeded by OCA on Sun Mar 30 20:40:40 2008
