1akl: Difference between revisions
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|PDB= 1akl |SIZE=350|CAPTION= <scene name='initialview01'>1akl</scene>, resolution 2.0Å | |PDB= 1akl |SIZE=350|CAPTION= <scene name='initialview01'>1akl</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1akl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1akl OCA], [http://www.ebi.ac.uk/pdbsum/1akl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1akl RCSB]</span> | |||
}} | }} | ||
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[[Category: Miyatake, H.]] | [[Category: Miyatake, H.]] | ||
[[Category: Morihara, K.]] | [[Category: Morihara, K.]] | ||
[[Category: hydrolase (metalloproteinase)]] | [[Category: hydrolase (metalloproteinase)]] | ||
''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 18:42:13 2008'' | ||
Revision as of 18:42, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Serralysin, with EC number 3.4.24.40 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080
OverviewOverview
The crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 has been determined at 2.0 A resolution by the X-ray method. The enzyme consists of N-terminal catalytic and C-terminal beta-helix domains. On structural comparison between the present unliganded enzyme and structurally- known liganded enzyme, some structural changes were observed around the active site. In the unliganded enzyme, Y216 serves as the fifth ligand for the active site zinc ion. On ligand binding, Y216 may move to form a hydrogen-bond with the carbonyl oxygen of the P1 residue of a ligand peptide. D191 in the flexible loop, Y190 to D196, over the active site cleft forms hydrogen-bonds with the backbone atoms of the P1 and P2 residues of the ligand to close the entrance to the cleft. The water molecule which is the fourth ligand for the zinc ion is replaced by the carbonyl oxygen of the P1 residue. These structural changes around the active site may reflect the substrate-binding mode during the enzymatic reaction.
About this StructureAbout this Structure
1AKL is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding., Miyatake H, Hata Y, Fujii T, Hamada K, Morihara K, Katsube Y, J Biochem. 1995 Sep;118(3):474-9. PMID:8690704
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