1UOK
CRYSTAL STRUCTURE OF B. CEREUS OLIGO-1,6-GLUCOSIDASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004556 | molecular_function | alpha-amylase activity |
A | 0004574 | molecular_function | oligo-1,6-glucosidase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0009313 | biological_process | oligosaccharide catabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | ASP199 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | GLU255 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O06994 |
Chain | Residue | Details |
A | ASP21 | |
A | ASN23 | |
A | ASP25 | |
A | ASP29 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000250 |
Chain | Residue | Details |
A | ASP329 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 8370659, 9193006, 10331869 |
Chain | Residue | Details |
A | ASP199 | |
A | ASP329 | |
A | GLU255 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 285 |
Chain | Residue | Details |
A | ASP98 | electrostatic destabiliser, electrostatic stabiliser, repulsive charge-charge interaction, steric role |
A | ASP199 | covalently attached, nucleofuge, nucleophile, polar interaction |
A | GLU255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, repulsive charge-charge interaction |
A | HIS328 | electrostatic stabiliser, hydrogen bond donor |
A | ASP329 | transition state stabiliser |