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4MAZ

The Structure of MalL mutant enzyme V200S 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 Residues12
DetailsBINDING SITE FOR RESIDUE TRS A 601
ChainResidue
AASP59
AHOH717
AHOH731
AHOH792
ATYR62
AHIS102
APHE144
APHE163
AASP199
AGLU255
AARG418
AGOL602

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
AGLU255
ALYS296
AASP332
AGLU389
AARG418
ATRS601
AHOH786
AHOH926

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 603
ChainResidue
AILE143
APRO293
ATRP297
AHOH812
AHOH943

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 604
ChainResidue
AASP20
AASN22
AASP24
APHE26
AASP28
AHOH867

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

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PDB entries from 2024-07-31

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