Brand  (β version)

PDB ID: 2FZS

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Ligands
Code Name Style Show Link
CMQ N~2~-[(benzyloxy)carbonyl]-N-[(1s,2s)-2-hydroxy-1-(4-hydroxybenzyl)propyl]-L-leucinamide PoSSuM
GOL Glycerol PoSSuM
PGE Triethylene glycol PoSSuM
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Structure summary

Code : 2FZS   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of E. coli ClpP with a Peptide Chloromethyl Ketone Covalently Bound at the Active Site
Release Data : 2006-05-23
Compound :
mol_id molecule chains synonym
1 ATP-dependent Clp protease proteolytic subunit A,B,C,D,E,F,G,H,I,J,K,L,M,N Endopeptidase Clp, Caseinolytic protease, Protease Ti, Heat shock protein F21.5
ec: 3.4.21.92
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli BL21(DE3)  (taxid:469008)
strain: K12, MG1655
gene: clpP, lopP
expression_system_strain: BL21 DE3
expression_system_vector_type: Plasmid
expression_system_plasmid: pET3d
Authors : Szyk, A., Maurizi, M.R.
Keywords : ATP-dependent ClpP protease, Z-Leu-Tyr Chloromethyl Ketone Inhibitor, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.90 Å )
Citation :

Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site.

Szyk, A.,Maurizi, M.R.
(2006)  J.Struct.Biol.  156 : 165 - 174

PubMed: 16682229
DOI: 10.1016/j.jsb.2006.03.013

Reaction

Chain : A, B, C, D, E, F, G, H, I, J, K, L, M, N
UniProt : P0A6G7 (CLPP_ECOLI)
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 HAMAP-Rule:MF_00444
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