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4MB1

The Structure of MalL mutant enzyme G202P from Bacillus subtilus

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
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS A 601
ChainResidue
AASP59
AHOH719
AHOH1179
ATYR62
AHIS102
APHE144
APHE163
AASP199
AGLU255
AARG418
AHOH717

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 602
ChainResidue
AASP20
AASN22
AASP24
APHE26
AASP28
AHOH822

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP199

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU255

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:24015933, ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1
ChainResidueDetails
AASP20
AASN22
AASP24
APHE26
AASP28

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP332

223166

PDB entries from 2024-07-31

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