Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3WY1

Crystal structure of alpha-glucosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004556molecular_functionalpha-amylase activity
A0004558molecular_functionalpha-1,4-glucosidase activity
A0005975biological_processcarbohydrate metabolic process
A0009313biological_processoligosaccharide catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
B0004556molecular_functionalpha-amylase activity
B0004558molecular_functionalpha-1,4-glucosidase activity
B0005975biological_processcarbohydrate metabolic process
B0009313biological_processoligosaccharide catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 600
ChainResidue
AASP23
AASP27
AVAL29
AASP31
AHOH934

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
AVAL173
APHE206
ATYR207
AHIS209
AASP243
AHOH728
ASER104
AVAL129
AASN165
AASP172

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PRU A 602
ChainResidue
AASP62
ATYR65
AHIS105
APHE147
APHE166
AARG200
AASP202
ATHR203
AGLY228
AGLU271
APHE297
AHIS332
AASP333
AARG400
AHOH704
AHOH816

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
BASP23
BASP27
BVAL29
BASP31
BHOH705

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PRU B 602
ChainResidue
BASP62
BTYR65
BHIS105
BILE146
BPHE147
BPHE166
BARG200
BASP202
BTHR203
BGLY228
BGLU271
BPHE297
BHIS332
BASP333
BARG400
BHOH748
BHOH924

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon