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4JKL

Crystal Structure of Streptococcus agalactiae beta-glucuronidase in space group P21212

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0004566molecular_functionbeta-glucuronidase activity
A0005102molecular_functionsignaling receptor binding
A0005615cellular_componentextracellular space
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019391biological_processglucuronoside catabolic process
A0030246molecular_functioncarbohydrate binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0004566molecular_functionbeta-glucuronidase activity
B0005102molecular_functionsignaling receptor binding
B0005615cellular_componentextracellular space
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0019391biological_processglucuronoside catabolic process
B0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AASP535
AHIS592

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 603
ChainResidue
AARG463
ATYR464
ATYR465
AHOH1051
AHOH1106

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
BARG463
BTYR465

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 Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P05804
ChainResidueDetails
AGLU408
BGLU408

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P05804
ChainResidueDetails
AGLU501
BGLU501

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P05804
ChainResidueDetails
AASP160
BASN462
BTYR468
BGLU501
BTRP546
BLYS565
AASN407
AASN462
ATYR468
AGLU501
ATRP546
ALYS565
BASP160
BASN407

220113

PDB entries from 2024-05-22

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