Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6LD0

Structure of Bifidobacterium dentium beta-glucuronidase complexed with C6-hexyl uronic isofagomine

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
A0030246molecular_functioncarbohydrate binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0004566molecular_functionbeta-glucuronidase activity
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0004565molecular_functionbeta-galactosidase activity
C0004566molecular_functionbeta-glucuronidase activity
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0030246molecular_functioncarbohydrate binding
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0004565molecular_functionbeta-galactosidase activity
D0004566molecular_functionbeta-glucuronidase activity
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue E8X A 701
ChainResidue
AASP179
AASN636
ALYS638
AHOH830
AHOH912
DASN157
AHIS413
AGLU479
AGLN519
ATYR539
ATYR543
AGLU574
ATRP619
AARG632

site_idAC2
Number of Residues15
Detailsbinding site for residue E8X B 701
ChainResidue
BMET153
BASP179
BHIS413
BGLU479
BGLN519
BTYR539
BTYR543
BGLU574
BTRP619
BARG632
BASN636
BLYS638
BHOH840
BHOH930
CASN157

site_idAC3
Number of Residues15
Detailsbinding site for residue E8X C 701
ChainResidue
BASN157
CASP179
CHIS413
CASN478
CGLU479
CGLN519
CTYR539
CTYR543
CGLU574
CTRP619
CARG632
CASN636
CLYS638
CHOH848
CHOH856

site_idAC4
Number of Residues14
Detailsbinding site for residue E8X D 701
ChainResidue
AASN157
DASP179
DHIS413
DGLU479
DGLN519
DTYR539
DTYR543
DGLU574
DTRP619
DARG632
DASN636
DLYS638
DHOH814
DHOH903

Functional Information from PROSITE/UniProt
site_idPS00608
Number of Residues15
DetailsGLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPCIVMWSia.NE
ChainResidueDetails
AASP465-GLU479

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsFRTSHYPyaesMYdlcDreGIVII
ChainResidueDetails
AASN407-ILE432

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon