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7PR6

Crystal structure of E. coli beta-glucuronidase in complex with covalent inhibitor ME727

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
AAA0004566molecular_functionbeta-glucuronidase activity
AAA0005829cellular_componentcytosol
AAA0005975biological_processcarbohydrate metabolic process
AAA0016798molecular_functionhydrolase activity, acting on glycosyl bonds
AAA0019391biological_processglucuronoside catabolic process
AAA0030246molecular_functioncarbohydrate binding
AAA0032991cellular_componentprotein-containing complex
AAA0042802molecular_functionidentical protein binding
BBB0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
BBB0004566molecular_functionbeta-glucuronidase activity
BBB0005829cellular_componentcytosol
BBB0005975biological_processcarbohydrate metabolic process
BBB0016798molecular_functionhydrolase activity, acting on glycosyl bonds
BBB0019391biological_processglucuronoside catabolic process
BBB0030246molecular_functioncarbohydrate binding
BBB0032991cellular_componentprotein-containing complex
BBB0042802molecular_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
AAAASP399-GLU413

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsYRTSHYPyaeeMLdwaDehGIVVI
ChainResidueDetails
AAAASN324-ILE349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21051639
ChainResidueDetails
AAAGLU413
BBBGLU413

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:35881786, ECO:0000305|PubMed:21051639
ChainResidueDetails
AAAGLU504
BBBGLU504

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000305|PubMed:21051639, ECO:0007744|PDB:3K4D
ChainResidueDetails
AAAASP163
BBBASN466
BBBTYR472
BBBGLU504
BBBTRP549
BBBLYS568
AAAASN412
AAAASN466
AAATYR472
AAAGLU504
AAATRP549
AAALYS568
BBBASP163
BBBASN412

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PDB entries from 2024-06-05

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