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4MVN

Crystal structure of the staphylococcal serine protease SplA in complex with a specific phosphonate inhibitor

Summary for 4MVN
Entry DOI10.2210/pdb4mvn/pdb
Related2W7U 3UFA 3W7S
DescriptorSerine protease splA, [(1S)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl]phosphonic acid (3 entities in total)
Functional Keywordschymotrypsin-like fold, serine endopeptidase, extracellular staphylococcal proteases, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceStaphylococcus aureus
Cellular locationSecreted: Q2FXC2
Total number of polymer chains4
Total formula weight88883.10
Authors
Zdzalik, M.,Burchacka, E.,Niemczyk, J.S.,Pustelny, K.,Popowicz, G.M.,Wladyka, B.,Dubin, A.,Potempa, J.,Sienczyk, M.,Dubin, G.,Oleksyszyn, J. (deposition date: 2013-09-24, release date: 2014-01-22, Last modification date: 2023-11-08)
Primary citationBurchacka, E.,Zdzalik, M.,Niemczyk, J.S.,Pustelny, K.,Popowicz, G.,Wladyka, B.,Dubin, A.,Potempa, J.,Sienczyk, M.,Dubin, G.,Oleksyszyn, J.
Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus.
Protein Sci., 23:179-189, 2014
Cited by
PubMed: 24375505
DOI: 10.1002/pro.2403
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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