1FFQ

CRYSTAL STRUCTURE OF CHITINASE A COMPLEXED WITH ALLOSAMIDIN

Summary for 1FFQ

• Entry DOI: 10.2210/pdb1ffq/pdb
• Related: 1CTN 1EDQ 1EHN 1EIB 1FFR
• Descriptor: CHITINASE A, 2-acetamido-2-deoxy-beta-D-allopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-allopyranose, ALLOSAMIZOLINE, ... (4 entities in total)
• Functional Keywords: glycosyl hydrolase, enzyme-inhibitor complex, hydrolase
• Biological source: Serratia marcescens
• Total number of polymer chains: 1
• Total formula weight: 59280.22

Authors

Papanikolau, Y.,Tavlas, G.,Vorgias, C.E.,Petratos, K. (deposition date: 2000-07-26, release date: 2003-02-11, Last modification date: 2024-11-06)

Primary citation

Papanikolau, Y.,Tavlas, G.,Vorgias, C.E.,Petratos, K.
De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin.
Acta Crystallogr.,Sect.D, 59:400-403, 2003

PubMed Abstract: The purification scheme of chitinase A (ChiA) from S. marcescens has been extensively revised. The pure enzyme crystallizes readily under new crystallization conditions. The ChiA crystal structure has been refined to 1.55 A resolution and the crystal structure of ChiA co-crystallized with the inhibitor allosamidin has been refined to 1.9 A resolution. Allosamidin is located in the deep active-site tunnel of ChiA and interacts with three important residues: Glu315, the proton donor of the catalysis, Asp313, which adopts two conformations in the native structure but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which lies opposite Glu315 in the active-site tunnel.

PubMed: 12554965
DOI: 10.1107/S0907444902021923

Experimental method

X-RAY DIFFRACTION (1.9 Å)