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5OSS

Beta-glucosidase from Thermotoga maritima in complex with Gluco-1H-imidazole

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue EDO A 501
ChainResidue
AALA54
ATYR421
AHOH650

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 502
ChainResidue
AALA144
AGLU145
AARG148
AHOH664

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 503
ChainResidue
ATRP142
ATHR90
ALYS131

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 504
ChainResidue
AGLY43
ALYS46
AALA407
AHOH702

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 505
ChainResidue
AARG240
ALYS337
AHOH603
AHOH609

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO A 506
ChainResidue
ATYR177
APHE267

site_idAC7
Number of Residues11
Detailsbinding site for residue EDO A 507
ChainResidue
AGLN20
AGLU166
ATYR295
ATRP324
AGLU351
ATRP398
AGLU405
ATRP406
APHE414
AHOH653
AHOH703

site_idAC8
Number of Residues2
Detailsbinding site for residue CL A 508
ChainResidue
AARG137
AHOH718

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO B 501
ChainResidue
BVAL53
BALA54
BTYR410
BTYR421
BHOH601

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO B 502
ChainResidue
AGLU110
BARG137
BARG199
BARG203
BASP279

site_idAD2
Number of Residues1
Detailsbinding site for residue EDO B 503
ChainResidue
BTYR177

site_idAD3
Number of Residues5
Detailsbinding site for residue NA B 504
ChainResidue
BASP278
BGLU282
BHOH627
BHOH712
BHOH735

site_idAD4
Number of Residues12
Detailsbinding site for residue AEZ B 505
ChainResidue
BGLN20
BHIS121
BASN165
BGLU166
BTYR295
BTRP324
BGLU351
BTRP398
BGLU405
BTRP406
BPHE414
BHOH614

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. VYITENGAA
ChainResidueDetails
AVAL347-ALA355

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGvAtASYQiEgS
ChainResidueDetails
APHE10-SER24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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