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Ligands
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EDO 1,2-ethanediol
FJT ~{N}-(1,3-benzodioxol-5-ylmethyl)-5-[(2-chloranyl-4-fluoranyl-phenyl)methyl]-1,3,4-oxadiazole-2-carboxamide
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Code : 6H23   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of the hClpP Y118A mutant with an activating small molecule
Release Data : 2018-08-29
Compound :
mol_id molecule chains synonym
1 ATP-dependent Clp protease proteolytic subunit, mitochondrial A,B,C,D,E,F,G,H,I,J,K,L,M,N Endopeptidase Clp
ec: 3.4.21.92
mutation: Y118A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
gene: CLPP
expression_system_variant: Rosetta2
Authors : Kick, L.M., Sieber, S.A., Schneider, S.
Keywords : protease, small molecule, 14mer, serine protease, oligomerization, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 3.089 Å )
Citation :

Selective Activation of Human Caseinolytic Protease P (ClpP).

Stahl, M.,Korotkov, V.S.,Balogh, D.  et al.
(2018)  Angew. Chem. Int. Ed. Engl.  57 : 14602 - 14607

PubMed: 30129683
DOI: 10.1002/anie.201808189

Chain : A, B, C, D, E, F, G, H, I, J, K, L, M, N
UniProt : Q16740 (CLPP_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
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 hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr- Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). 3.4.21.92 PubMed:11923310, PubMed:15522782, PubMed:22354088
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