1VFO
Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/beta-cyclodextrin complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0031216 | molecular_function | neopullulanase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0031216 | molecular_function | neopullulanase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P38940 |
| Chain | Residue | Details |
| A | ASN325 | |
| B | ASN325 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P38940 |
| Chain | Residue | Details |
| A | GLU354 | |
| B | GLU354 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2 |
| Chain | Residue | Details |
| A | ASN143 | |
| B | ASP149 | |
| B | GLY169 | |
| B | ASP171 | |
| A | ASP145 | |
| A | ASN148 | |
| A | ASP149 | |
| A | GLY169 | |
| A | ASP171 | |
| B | ASN143 | |
| B | ASP145 | |
| B | ASN148 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P38940 |
| Chain | Residue | Details |
| A | HIS244 | |
| B | ARG469 | |
| A | ARG323 | |
| A | HIS420 | |
| A | ASP465 | |
| A | ARG469 | |
| B | HIS244 | |
| B | ARG323 | |
| B | HIS420 | |
| B | ASP465 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN421 | |
| B | ASN421 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | TRP356 | |
| A | ASN325 | |
| A | ASN421 | |
| A | GLU354 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | TRP356 | |
| B | ASN325 | |
| B | ASN421 | |
| B | GLU354 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASN421 | |
| A | ASN325 | |
| A | GLU354 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASN421 | |
| B | ASN325 | |
| B | GLU354 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASN325 | |
| A | GLU354 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASN325 | |
| B | GLU354 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 433 |
| Chain | Residue | Details |
| A | ASN325 | covalent catalysis |
| A | GLU354 | proton shuttle (general acid/base) |
| A | ASN421 | transition state stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 433 |
| Chain | Residue | Details |
| B | ASN325 | covalent catalysis |
| B | GLU354 | proton shuttle (general acid/base) |
| B | ASN421 | transition state stabiliser |
