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6LEM

Structure of E. coli beta-glucuronidase complex with C6-nonyl uronic isofagomine

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
A0019391biological_processglucuronoside catabolic process
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
B0019391biological_processglucuronoside catabolic process
B0030246molecular_functioncarbohydrate binding
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue E9O A 701
ChainResidue
AASP163
AASN566
ALYS568
AHIS330
AGLU413
APHE448
ATYR468
ATYR472
AGLU504
ATRP549
AARG562

site_idAC2
Number of Residues10
Detailsbinding site for residue E9O B 701
ChainResidue
BASP163
BHIS330
BLEU361
BGLU413
BTYR472
BGLU504
BTRP549
BARG562
BASN566
BLYS568

Functional Information from PROSITE/UniProt
site_idPS00608
Number of Residues15
DetailsGLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPSVVMWSia.NE
ChainResidueDetails
BASP399-GLU413
AASP399-GLU413

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsYRTSHYPyaeeMLdwaDehGIVVI
ChainResidueDetails
BASN324-ILE349
AASN324-ILE349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21051639
ChainResidueDetails
BGLU413

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:35881786, ECO:0000305|PubMed:21051639
ChainResidueDetails
BGLU504

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000305|PubMed:21051639, ECO:0007744|PDB:3K4D
ChainResidueDetails
BASP163
BASN412
BASN466
BTYR472
BGLU504
BTRP549
BLYS568

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PDB entries from 2024-08-07

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