2XLN

Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor

Summary for 2XLN

Entry DOI	10.2210/pdb2xln/pdb
Related	1W79 1W8Q 1W8Y 2VGJ 2VGK 2WKE 2XDM 2XK1 2Y4A 2Y55 2Y59
Descriptor	D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,, [(1S)-1-{[(2,6-DIMETHOXYPHENYL)CARBONYL]AMINO}ETHYL]BORONIC ACID, SULFATE ION, ... (5 entities in total)
Functional Keywords	hydrolase, peptidoglycan
Biological source	ACTINOMADURA SP
Cellular location	Secreted: P39045
Total number of polymer chains	4
Total formula weight	203098.42
Authors	Sauvage, E.,Herman, R.,Kerff, F.,Rocaboy, M.,Charlier, P. (deposition date: 2010-07-21, release date: 2011-01-26, Last modification date: 2014-06-18)
Primary citation	Woon, E.C.Y.,Zervosen, A.,Sauvage, E.,Simmons, K.J.,Ivec, M.,Inglis, S.R.,Fishwick, C.W.G.,Gobec, S.,Charlier, P.,Luxen, A.,Schofield, C.J. Structure Guided Development of Potent Reversibly Binding Penicillin Binding Protein Inhibitors Acs Med.Chem.Lett., 2:219-, 2011 Cited by PubMed Abstract: Following from the evaluation of different types of electrophiles, combined modeling and crystallographic analyses are used to generate potent boronic acid based inhibitors of a penicillin binding protein. The results suggest that a structurally informed approach to penicillin binding protein inhibition will be useful for the development of both improved reversibly binding inhibitors, including boronic acids, and acylating inhibitors, such as β-lactams. PubMed: 24900305 DOI: 10.1021/ML100260X PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.4 Å)

Structure validation