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3ABZ

Crystal structure of Se-Met labeled Beta-glucosidase from Kluyveromyces marxianus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0102483molecular_functionscopolin beta-glucosidase activity
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
B0102483molecular_functionscopolin beta-glucosidase activity
C0000272biological_processpolysaccharide catabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0008422molecular_functionbeta-glucosidase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0030245biological_processcellulose catabolic process
C0102483molecular_functionscopolin beta-glucosidase activity
D0000272biological_processpolysaccharide catabolic process
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0008422molecular_functionbeta-glucosidase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0030245biological_processcellulose catabolic process
D0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 5001
ChainResidue
ATRP28
AASP45
ALYS146
AMSE190
AASP225
ATRP226
ASER356
AHOH1983
AHOH2266

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 5002
ChainResidue
APHE55
APHE56
AASP57
AGLY58
AVAL437
AARG439
AASN441
AHOH1152
AHOH1855

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 5003
ChainResidue
ALYS665
AGLY715
ATYR716
AGLY717
ATHR823
ASER824
AASP827
AHOH1130
AHOH1886

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 5004
ChainResidue
AGLN137
AALA184
AASN185
AHOH2285
AHOH2674
AHOH2727
AHOH2749

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 5005
ChainResidue
BASP45
BLYS146
BMSE190
BASP225
BTRP226
BSER356
BHOH961
BHOH2365

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 5006
ChainResidue
BPHE56
BASP57
BVAL437
BASN438
BARG439
BASN441
BVAL442
BHOH1246

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 5007
ChainResidue
CASP45
CLEU99
CLYS146
CMSE190
CASP225
CTRP226
CSER356
CHOH1203
CHOH1830

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL D 5008
ChainResidue
DTRP28
DASP45
DLEU99
DLYS146
DMSE190
DASP225
DTRP226
DHOH1360

Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. ILRdEwkwdGMLMSDwfG
ChainResidueDetails
AILE211-GLY228

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PDB entries from 2024-07-31

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