2E40
Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium in complex with gluconolactone
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008422 | molecular_function | beta-glucosidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0030245 | biological_process | cellulose catabolic process |
A | 0080079 | molecular_function | cellobiose glucosidase activity |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008422 | molecular_function | beta-glucosidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0030245 | biological_process | cellulose catabolic process |
B | 0080079 | molecular_function | cellobiose glucosidase activity |
Functional Information from PROSITE/UniProt
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FvWGyAtAAYQiEgS |
Chain | Residue | Details |
A | PHE10-SER24 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:17376440 |
Chain | Residue | Details |
A | GLU170 | |
B | GLU170 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:17376440 |
Chain | Residue | Details |
A | GLU365 | |
B | GLU365 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17376440 |
Chain | Residue | Details |
A | GLN20 | |
B | TRP415 | |
A | HIS123 | |
A | ASN169 | |
A | TYR301 | |
A | TRP415 | |
B | GLN20 | |
B | HIS123 | |
B | ASN169 | |
B | TYR301 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU422 | |
B | GLU422 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1cbg |
Chain | Residue | Details |
A | GLU170 | |
A | GLU365 | |
A | ASN299 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1cbg |
Chain | Residue | Details |
B | GLU170 | |
B | GLU365 | |
B | ASN299 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cbg |
Chain | Residue | Details |
A | GLU170 | |
A | GLU365 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cbg |
Chain | Residue | Details |
B | GLU170 | |
B | GLU365 |