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1GPF

CHITINASE B FROM SERRATIA MARCESCENS IN COMPLEX WITH INHIBITOR PSAMMAPLIN

Summary for 1GPF
Entry DOI10.2210/pdb1gpf/pdb
Related1E15 1E6N 1E6P 1E6R 1E6Z 1GOI
DescriptorCHITINASE B, SULFATE ION (3 entities in total)
Functional Keywordshydrolase, chitin degradation, inhibitor psammaplin
Biological sourceSERRATIA MARCESCENS
Total number of polymer chains2
Total formula weight111324.21
Authors
Komander, D.,Van Aalten, D.M. (deposition date: 2001-11-03, release date: 2002-10-31, Last modification date: 2024-10-23)
Primary citationTabudravu, J.N.,Eijsink, V.G.,Gooday, G.W.,Jaspars, M.,Komander, D.,Legg, M.,Synstad, B.,Van Aalten, D.M.
Psammaplin A, a Chitinase Inhibitor Isolated from the Fijian Marine Sponge Aplysinella Rhax
Bioorg.Med.Chem., 10:1123-, 2002
Cited by
PubMed Abstract: Several brominated tyrosine derived compounds, psammaplins A (1), K (2) and L (3) as well as bisaprasin (4) were isolated from the Fijian marine sponge Aplysinella rhax during a bioassay guided isolation protocol. Their structures were determined using NMR and MS techniques. Psammaplin A was found to moderately inhibit chitinase B from Serratia marcescens, the mode of inhibition being non-competitive. Crystallographic studies suggest that a disordered psammaplin A molecule is bound near the active site. Interestingly, psammaplin A was found to be a potent antifungal agent.
PubMed: 11836123
DOI: 10.1016/S0968-0896(01)00372-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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