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5IXE

1.75A RESOLUTION STRUCTURE OF 5-Fluoroindole BOUND BETA-GLYCOSIDASE (W33G) FROM SULFOLOBUS SOLFATARICUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0008378molecular_functiongalactosyltransferase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0005975biological_processcarbohydrate metabolic process
B0008378molecular_functiongalactosyltransferase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue 14O A 501
ChainResidue
AGLY33
AVAL37
ATRP151
APRO152
AGLY221
APHE222
APRO223
ATRP433
AALA434

site_idAC2
Number of Residues8
Detailsbinding site for residue MPD A 502
ChainResidue
APRO89
AASN90
ATYR121
AASN123
AHOH655
AHOH718
AHOH784
BTHR450

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 503
ChainResidue
AASN264
ASER265
AARG286
AHOH767

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 504
ChainResidue
AARG440
ATYR448

site_idAC5
Number of Residues2
Detailsbinding site for residue CL A 505
ChainResidue
AARG295
AHOH727

site_idAC6
Number of Residues9
Detailsbinding site for residue 14O B 501
ChainResidue
BGLY33
BVAL37
BTRP151
BPRO152
BGLY221
BPHE222
BPRO223
BTRP433
BALA434

site_idAC7
Number of Residues4
Detailsbinding site for residue CL B 502
ChainResidue
BASN264
BSER265
BARG286
BHOH742

site_idAC8
Number of Residues1
Detailsbinding site for residue CL B 503
ChainResidue
BARG295

site_idAC9
Number of Residues2
Detailsbinding site for residue CL B 504
ChainResidue
BARG440
BTYR448

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. MYVTENGIA
ChainResidueDetails
AMET383-ALA391

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FrFGwSqAGFQsEmG
ChainResidueDetails
APHE8-GLY22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AGLU206
BGLU206

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
ChainResidueDetails
AGLU387
BGLU387

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Not N6-methylated
ChainResidueDetails
ALYS76
ALYS102
ALYS124
ALYS138
BLYS76
BLYS102
BLYS124
BLYS138

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:14660666
ChainResidueDetails
ALYS116
ALYS273
ALYS311
BLYS116
BLYS273
BLYS311

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-methyllysine => ECO:0000269|PubMed:14660666
ChainResidueDetails
ALYS135
ALYS332
BLYS135
BLYS332

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PDB entries from 2025-06-18

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