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1EHN

CRYSTAL STRUCTURE OF CHITINASE A MUTANT E315Q COMPLEXED WITH OCTA-N-ACETYLCHITOOCTAOSE (NAG)8.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004568molecular_functionchitinase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0008061molecular_functionchitin binding
A0008152biological_processmetabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLN315

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 478
ChainResidueDetails
AASP311electrostatic stabiliser
AASP313steric role
AGLN315proton shuttle (general acid/base)
ATYR390electrostatic destabiliser

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PDB entries from 2024-04-24

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