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4ZE5

Structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016052biological_processcarbohydrate catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033920molecular_function6-phospho-beta-galactosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033920molecular_function6-phospho-beta-galactosidase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0008422molecular_functionbeta-glucosidase activity
C0016052biological_processcarbohydrate catabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0033920molecular_function6-phospho-beta-galactosidase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0008422molecular_functionbeta-glucosidase activity
D0016052biological_processcarbohydrate catabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0033920molecular_function6-phospho-beta-galactosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 501
ChainResidue
ATRP260
AARG369
AGLN371
AGOL502
AHOH853
AHOH921

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 502
ChainResidue
AHOH913
ATRP260
AMET262
AGOL501

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 503
ChainResidue
ATYR263
AGLN265
ATRP268
AHOH964

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 504
ChainResidue
AASN245
AALA266
ALEU336
AHOH609
AHOH615
AHOH893

site_idAC5
Number of Residues5
Detailsbinding site for residue IMD A 505
ChainResidue
AASP59
AARG63
AGLU453
AHOH603
AHOH1070

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL B 501
ChainResidue
BTRP260
BMET262
BGOL502
BHOH904

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL B 502
ChainResidue
BTRP260
BARG369
BGLN371
BGOL501
BHOH895

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 503
ChainResidue
BTYR263
BGLN265
BTRP268
BTRP285

site_idAC9
Number of Residues3
Detailsbinding site for residue GOL C 501
ChainResidue
CTYR233
CHIS344
CHOH940

site_idAD1
Number of Residues7
Detailsbinding site for residue GOL C 502
ChainResidue
CTYR263
CPRO264
CGLN265
CTRP268
CTRP285
CHOH806
CHOH1015

site_idAD2
Number of Residues4
Detailsbinding site for residue IMD C 503
ChainResidue
AHOH629
CLYS189
CASP190
CHOH911

site_idAD3
Number of Residues4
Detailsbinding site for residue GOL D 501
ChainResidue
DTYR263
DPRO264
DGLN265
DTRP285

site_idAD4
Number of Residues5
Detailsbinding site for residue IMD D 502
ChainResidue
CPRO343
CHIS344
CVAL345
CASP346
DARG157

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. ILITENGLG
ChainResidueDetails
AILE374-GLY382

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGaAsAAYQvEgA
ChainResidueDetails
APHE13-ALA27

219869

PDB entries from 2024-05-15

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