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4EAM

1.70A resolution structure of apo 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
A0008422molecular_functionbeta-glucosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
AASN264
ASER265
AARG286
AHOH723

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 502
ChainResidue
AARG440
AVAL446
ATYR448

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AARG295
AHOH712

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD A 504
ChainResidue
APRO89
AASN90
ATYR121
AASN123
AHOH625
AHOH629
BTHR450
BHOH720

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 505
ChainResidue
AGLU206
ASER265
ATYR322
ATRS507
AHOH618

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 506
ChainResidue
ASER220
AGLU432
ATRP433
AALA434
AHOH695

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS A 507
ChainResidue
AGLN18
AGLU206
ATYR322
ATRP361
AGLU387
ATRP425
AGLU432
AMPD505
AHOH670

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 501
ChainResidue
BASN264
BSER265
BARG286

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 502
ChainResidue
BARG295
BHOH768
BHOH884

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 503
ChainResidue
BARG440
BTYR448
BHOH888

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD B 504
ChainResidue
BGLU206
BSER265
BTYR322
BTRS507
BHOH617
BHOH891

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD B 505
ChainResidue
APRO29
AHOH757
BPRO24
BGLY25
BTRP60
BASP125
BHOH896

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 506
ChainResidue
BSER220
BGLU432
BTRP433
BALA434

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS B 507
ChainResidue
BGLN18
BGLU206
BTYR322
BTRP361
BGLU387
BTRP425
BGLU432
BMPD504
BHOH695

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 2024-05-15

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