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PDBsum entry 7dft
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PDB id:
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Hydrolase
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Title:
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Crystal structure of xanthomonas oryzae clpp
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Structure:
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Atp-dependent clp protease proteolytic subunit. Chain: a, b, c, d, e, f, g. Synonym: endopeptidase clp. Engineered: yes
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Source:
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Xanthomonas oryzae. Organism_taxid: 347. Gene: clpp, adt25_23080, adt27_15185, eyr26_04825. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.80Å
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R-factor:
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0.188
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R-free:
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0.222
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Authors:
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C.-G.Yang,T.Yang
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Key ref:
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C.-G.Yang
and
t.yang
Crystal structure of caseinolytic protease p.
To be published,
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PubMed id:
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Date:
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09-Nov-20
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Release date:
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19-May-21
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PROCHECK
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Headers
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References
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Q5H434
(CLPP_XANOR) -
ATP-dependent Clp protease proteolytic subunit from Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
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Seq: Struc:
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208 a.a.
180 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.3.4.21.92
- endopeptidase Clp.
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Reaction:
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Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are cleaved (such as succinyl-Leu-Tyr-|-NHMEC; and Leu-Tyr-Leu-|-Tyr-Trp, in which the cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp- bond also occurs).
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');
}
}
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