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7Q9H

Peptide LLKAVAEKQ in complex with human cathepsin V C25A mutant

This is a non-PDB format compatible entry.
Summary for 7Q9H
Entry DOI10.2210/pdb7q9h/pdb
DescriptorCathepsin L2, LLKAVAEKQ Peptide, CHLORIDE ION, ... (6 entities in total)
Functional Keywordscathepsinv, peptidyl substrate, hydrolase
Biological sourceHomo sapiens (Human)
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Total number of polymer chains5
Total formula weight52549.17
Authors
Loboda, J.,Sosnowski, P.,Tusar, L.,Vidmar, R.,Vizovisek, M.,Horvat, J.,Kosec, G.,Impens, F.,Demol, H.,Turk, B.,Gevaert, K.,Turk, D. (deposition date: 2021-11-12, release date: 2022-11-23, Last modification date: 2024-02-07)
Primary citationTusar, L.,Loboda, J.,Impens, F.,Sosnowski, P.,Van Quickelberghe, E.,Vidmar, R.,Demol, H.,Sedeyn, K.,Saelens, X.,Vizovisek, M.,Mihelic, M.,Fonovic, M.,Horvat, J.,Kosec, G.,Turk, B.,Gevaert, K.,Turk, D.
Proteomic data and structure analysis combined reveal interplay of structural rigidity and flexibility on selectivity of cysteine cathepsins.
Commun Biol, 6:450-450, 2023
Cited by
PubMed: 37095140
DOI: 10.1038/s42003-023-04772-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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