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3CMG

Crystal structure of putative beta-galactosidase from Bacteroides fragilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 810
ChainResidue
AHIS359
AASN428
AGLU429
AASN477
AGLU510
ATRP562
AHOH937
AHOH1007
AHOH1010

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 820
ChainResidue
ALYS392
AGLY393
APHE394
ALYS431

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 801
ChainResidue
AALA222
AGLY224
ATHR225
ALYS285

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 802
ChainResidue
APHE49
AARG60
AHIS66
AHOH994
AHOH1196
AHOH1306

Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues119
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mslrqdillnnnwnfrfshqvqgdtrrvdlphtwnaqdalagkidykrgignyekalyirpewkgkrlflrfdgvnsiadvfinrkhigehrggygafifeitdlvkygek....NSVLVRAN
ChainResidueDetails
AMET35-ASN153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P05804
ChainResidueDetails
AGLU429

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P05804
ChainResidueDetails
AASN428
AASN477
ATYR483
ATRP562
ALYS583

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bgl
ChainResidueDetails
AGLU510
AGLU429

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bgl
ChainResidueDetails
AGLU510
ATYR479
AGLU429

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PDB entries from 2024-07-31

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