1BVZ
ALPHA-AMYLASE II (TVAII) FROM THERMOACTINOMYCES VULGARIS R-47
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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 0016787 | molecular_function | hydrolase activity |
| 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 | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P38940","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P38940","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12051850","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JI2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P38940","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 12051850 |
| Chain | Residue | Details |
| A | TRP356 | |
| A | ASP325 | |
| A | ASP421 | |
| A | GLU354 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 12051850 |
| Chain | Residue | Details |
| B | TRP356 | |
| B | ASP325 | |
| B | ASP421 | |
| B | GLU354 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 433 |
| Chain | Residue | Details |
| A | ASP325 | covalent catalysis |
| A | GLU354 | proton shuttle (general acid/base) |
| A | ASP421 | transition state stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 433 |
| Chain | Residue | Details |
| B | ASP325 | covalent catalysis |
| B | GLU354 | proton shuttle (general acid/base) |
| B | ASP421 | transition state stabiliser |
