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7M1R

Crystal structure of a 6-phospho-beta-galactosidase from Bacillus licheniformis

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
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
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue EDO A 501
ChainResidue
ATYR123
AASN174
APRO185
AHOH708
AHOH721

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 502
ChainResidue
AHOH705
AGLU170
ATYR173
ATYR301
AHOH682

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 503
ChainResidue
AARG93
ATYR135
AARG142
AGLU145
AASP146
AHOH789

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO B 501
ChainResidue
BTYR123
BASN174
BPRO185
BHOH701
BHOH799

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO B 502
ChainResidue
BGLU170
BTYR173
BTYR301
BHOH729
BHOH761

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO B 503
ChainResidue
BARG93
BTYR135
BARG142
BGLU145
BASP146
BHOH636
BHOH834

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO C 501
ChainResidue
CTYR123
CASN174
CPHE175
CPRO185
CHOH684
CHOH741

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO C 502
ChainResidue
CGLU170
CTYR173
CTYR301
CHOH690
CHOH783

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO C 503
ChainResidue
CARG93
CARG142
CGLU145
CASP146
CHOH760

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO D 501
ChainResidue
DGLU170
DTYR173
DTYR301
DTRP352
DHOH638

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LFITENGLG
ChainResidueDetails
ALEU374-GLY382

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

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PDB entries from 2024-06-12

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