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4JKK

Crystal Structure of Streptococcus agalactiae beta-glucuronidase in space group I222

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0004566molecular_functionbeta-glucuronidase activity
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019391biological_processglucuronoside catabolic process
A0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AGLY372
AGLY372
ATRP374
ATRP374

Functional Information from PROSITE/UniProt
site_idPS00608
Number of Residues15
DetailsGLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPSVVMWVva.NE
ChainResidueDetails
AASP394-GLU408

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsFRTSHYPyseeMMrlaDrmGVLVI
ChainResidueDetails
AASN323-ILE348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P05804
ChainResidueDetails
AGLU408

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P05804
ChainResidueDetails
AGLU501

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P05804
ChainResidueDetails
AASP160
AASN407
AASN462
ATYR468
AGLU501
ATRP546
ALYS565

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PDB entries from 2024-07-17

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