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5WDK

A processive dipeptidyl aminopeptidase secreted from an established commensal bacterium P. distasonis

Summary for 5WDK
Entry DOI10.2210/pdb5wdk/pdb
DescriptorAminopeptidase C, POTASSIUM ION, 5-[(3aS,4R,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-N-(2-oxopropyl)pentanamide, ... (4 entities in total)
Functional Keywordsprotease, hydrolase
Biological sourceParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)
Total number of polymer chains6
Total formula weight277598.61
Authors
Wolan, D.W.,Xu, J.H.,Solania, A.,Chatterjee, S.,Jiang, Z.,ODonoghue, A.J. (deposition date: 2017-07-05, release date: 2018-07-11, Last modification date: 2023-10-04)
Primary citationXu, J.H.,Jiang, Z.,Solania, A.,Chatterjee, S.,Suzuki, B.,Lietz, C.B.,Hook, V.Y.H.,O'Donoghue, A.J.,Wolan, D.W.
A Commensal Dipeptidyl Aminopeptidase with Specificity for N-Terminal Glycine Degrades Human-Produced Antimicrobial Peptides in Vitro.
Acs Chem.Biol., 13:2513-2521, 2018
Cited by
PubMed: 30085657
DOI: 10.1021/acschembio.8b00420
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.36 Å)
Structure validation

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