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1PBG

THE THREE-DIMENSIONAL STRUCTURE OF 6-PHOSPHO-BETA GALACTOSIDASE FROM LACTOCOCCUS LACTIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0005990biological_processlactose catabolic process
A0008152biological_processmetabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019512biological_processlactose catabolic process via tagatose-6-phosphate
A0033920molecular_function6-phospho-beta-galactosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0005990biological_processlactose catabolic process
B0008152biological_processmetabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0019512biological_processlactose catabolic process via tagatose-6-phosphate
B0033920molecular_function6-phospho-beta-galactosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 469
ChainResidue
ASER428
ALYS435
AHOH644

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 469
ChainResidue
BSER428
BSER430
BASN431
BTYR437

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGLG
ChainResidueDetails
AILE371-GLY379

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FiFGgAtAAYQaEgA
ChainResidueDetails
APHE9-ALA23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000305|PubMed:8535789
ChainResidueDetails
AGLU160
BGLU160

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000305|PubMed:8535789
ChainResidueDetails
AGLU375
BGLU375

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG
ChainResidueDetails
AGLN19
BGLN19
BHIS116
BASN159
BGLU160
BASN297
BSER428
BTRP429
BLYS435
BTYR437
AHIS116
AASN159
AGLU160
AASN297
ASER428
ATRP429
ALYS435
ATYR437

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 877
ChainResidueDetails
AGLU160proton shuttle (general acid/base)
AGLU375covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 877
ChainResidueDetails
BGLU160proton shuttle (general acid/base)
BGLU375covalent catalysis

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PDB entries from 2024-03-27

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