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3BGA

Crystal structure of beta-galactosidase from Bacteroides thetaiotaomicron VPI-5482

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0005990biological_processlactose catabolic process
A0009341cellular_componentbeta-galactosidase complex
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0005975biological_processcarbohydrate metabolic process
B0005990biological_processlactose catabolic process
B0009341cellular_componentbeta-galactosidase complex
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1
ChainResidue
AGLU438
AHIS440
AGLU484
AHOH1476
AHOH1477
AHOH1478

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 2
ChainResidue
BHOH1462
BHOH1463
BHOH1465
BGLU438
BHIS440
BGLU484

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 3
ChainResidue
BASP227
BPHE614
BASN617
BHOH1039
BHOH1603

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 4
ChainResidue
AASP227
APHE614
AASN617
AHOH1054
AHOH1589

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 5
ChainResidue
BPRO924
BLEU966
BGLU967
BALA969
BHOH1470
BHOH1547

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 6
ChainResidue
APRO924
ALEU966
AGLU967
AALA969
AHOH1099
AHOH1520

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 7
ChainResidue
ALYS192
ATHR193
AASN436
AHOH1179

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 8
ChainResidue
BLYS192
BTHR193
BASN436

Functional Information from PROSITE/UniProt
site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NmVRNSHYPthpyWYqlcDryGLYMI
ChainResidueDetails
AASN407-ILE432

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bgl
ChainResidueDetails
AGLU548
AGLU484

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bgl
ChainResidueDetails
BGLU548
BGLU484

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bgl
ChainResidueDetails
ATYR521
AGLU548
AGLU484

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bgl
ChainResidueDetails
BTYR521
BGLU548
BGLU484

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PDB entries from 2024-07-24

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