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3ZSS

Apo form of GlgE isoform 1 from Streptomyces coelicolor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004556molecular_functionalpha-amylase activity
A0005975biological_processcarbohydrate metabolic process
A0009313biological_processoligosaccharide catabolic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016758molecular_functionhexosyltransferase activity
A0030979biological_processalpha-glucan biosynthetic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004556molecular_functionalpha-amylase activity
B0005975biological_processcarbohydrate metabolic process
B0009313biological_processoligosaccharide catabolic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016758molecular_functionhexosyltransferase activity
B0030979biological_processalpha-glucan biosynthetic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0004556molecular_functionalpha-amylase activity
C0005975biological_processcarbohydrate metabolic process
C0009313biological_processoligosaccharide catabolic process
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0016758molecular_functionhexosyltransferase activity
C0030979biological_processalpha-glucan biosynthetic process
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0004556molecular_functionalpha-amylase activity
D0005975biological_processcarbohydrate metabolic process
D0009313biological_processoligosaccharide catabolic process
D0016740molecular_functiontransferase activity
D0016757molecular_functionglycosyltransferase activity
D0016758molecular_functionhexosyltransferase activity
D0030979biological_processalpha-glucan biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues70
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mgsshhhhhhssglvprgshmpathhssatsaerptvvgripvldvrpvvqrgrrpakavtg.....................................................ESFEVSAT
ChainResidueDetails
AMET-19-THR50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21914799","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21914799","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21914799","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"21914799","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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