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6EFU

Crystal structure of the double mutant L167W / P172L of the beta-glucosidase from Trichoderma harzianum

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
A0016787molecular_functionhydrolase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue NO3 A 501
ChainResidue
ATRP338
ANO3502

site_idAC2
Number of Residues7
Detailsbinding site for residue NO3 A 502
ChainResidue
ATYR297
AGLU366
ATRP416
AGLU423
APHE432
ANO3501
AHOH608

site_idAC3
Number of Residues4
Detailsbinding site for residue NO3 B 501
ChainResidue
BSER185
BTHR186
BTHR187
BHOH681

site_idAC4
Number of Residues2
Detailsbinding site for residue NO3 B 502
ChainResidue
BTRP338
BHOH712

site_idAC5
Number of Residues5
Detailsbinding site for residue NO3 B 503
ChainResidue
BTYR297
BGLU366
BGLU423
BTRP424
BHOH708

Functional Information from PROSITE/UniProt
site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FqWGfAtAAYQiEgA
ChainResidueDetails
APHE6-ALA20

217705

PDB entries from 2024-03-27

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