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3K46

Crystal structure of full-length E. coli beta-glucuronidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004566molecular_functionbeta-glucuronidase activity
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004566molecular_functionbeta-glucuronidase activity
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
Functional Information from PROSITE/UniProt
site_idPS00608
Number of Residues15
DetailsGLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPSVVMWSia.NE
ChainResidueDetails
AASP399-GLU413

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsYRTSHYPyaeeMLdwaDehGIVVI
ChainResidueDetails
AASN324-ILE349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21051639
ChainResidueDetails
AGLU413
BGLU413

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:35881786, ECO:0000305|PubMed:21051639
ChainResidueDetails
AGLU504
BGLU504

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000305|PubMed:21051639, ECO:0007744|PDB:3K4D
ChainResidueDetails
AASP163
BASN466
BTYR472
BGLU504
BTRP549
BLYS568
AASN412
AASN466
ATYR472
AGLU504
ATRP549
ALYS568
BASP163
BASN412

227344

PDB entries from 2024-11-13

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