spacer

PDBe Entry: 2zl2 view

Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.5 Å, R-factor: 23.0%, Free R-factor: 27.4%, Spacegroup: P 21 21 21
Released 22/04/2008, deposition: 02/04/2008, last revision: 24/02/2009
Authors Kim, D.Y.search; Kim, K.K.search
Primary citation The structural basis for the activation and peptide recognition of bacterial ClpP
J.MOL.BIOL.search vol:379, pag:760-771 (2008) [PubMed ID 18468623 ]search
Keywords Peptide substratesearch, Cytoplasmsearch, Hydrolasesearch, Proteasesearch, Serine proteasesearch
EC 3.4.21.92 ExPASy BRENDA search (A B C D E F G H I J K L M N)
Organism Helicobacter pylori 210search(A B C D E F G H I J K L M N)
UniProt ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Endopeptidase Clp) P56156search (A B C D E F G H I J K L M N)
Related entries 2zl0, 2zl2, 2zl3
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D, E, F, G, H, I, J, K, L, M, N ATP-dependent Clp protease proteolytic subunit Protein P56156 (CLPP_HELPY)search
196 88%
O, P, Q, T, U, V, W, X A peptide substrate-NVLGFTQ Protein
7 57%
R, S A peptide substrate-NVLGFTQ for Chain R and S Protein
7 57%
spacer