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4M56

The Structure of Wild-type MalL from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004556molecular_functionalpha-amylase activity
A0004574molecular_functionoligo-1,6-glucosidase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0009313biological_processoligosaccharide catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
B0004556molecular_functionalpha-amylase activity
B0004574molecular_functionoligo-1,6-glucosidase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0009313biological_processoligosaccharide catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP199
BASP199

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU255
BGLU255

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:24015933, ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1
ChainResidueDetails
AASP20
BASP28
AASN22
AASP24
APHE26
AASP28
BASP20
BASN22
BASP24
BPHE26

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP332
BASP332

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PDB entries from 2024-07-31

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