1gtj
From Proteopedia
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|PDB= 1gtj |SIZE=350|CAPTION= <scene name='initialview01'>1gtj</scene>, resolution 1.75Å | |PDB= 1gtj |SIZE=350|CAPTION= <scene name='initialview01'>1gtj</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=AC1:Ace+Binding+Site+For+Chain+2'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ace+Binding+Site+For+Chain+2'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gtj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtj OCA], [http://www.ebi.ac.uk/pdbsum/1gtj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gtj RCSB]</span> | ||
}} | }} | ||
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[[Category: Oyama, H.]] | [[Category: Oyama, H.]] | ||
[[Category: Uchida, K.]] | [[Category: Uchida, K.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: SO4]] | ||
[[Category: serine-carboxyl type proteinase]] | [[Category: serine-carboxyl type proteinase]] | ||
[[Category: thermostable]] | [[Category: thermostable]] | ||
| - | ''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 20:50:56 2008'' |
Revision as of 17:50, 30 March 2008
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| , resolution 1.75Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)- COMPLEX WITH AC-ILE-ALA-PHE-CHO
Overview
Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine-carboxyl proteinases, which also includes CLN2, a human lysosomal homolog recently implicated in a fatal neurodegenerative disease. Kumamolysin and its complexes with two aldehyde inhibitors were crystallized, and their three-dimensional structures were solved and refined with X-ray data to 1.4 A resolution. As its Pseudomonas homolog, kumamolysin exhibits a Ser/Glu/Asp catalytic triad with particularly short interconnecting hydrogen bonds and an oxyanion hole enabling the reactive serine to attack substrate peptide bonds at quite acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might further facilitate proton delocalization during nucleophilic attack, in particular at high temperature.
About this Structure
1GTJ is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
Reference
The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase., Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W, Structure. 2002 Jun;10(6):865-76. PMID:12057200
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