5Z0T
Thermoactinomyces vulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005576 | cellular_component | extracellular region |
| 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 | 0005576 | cellular_component | extracellular region |
| 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 PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 701 |
| Chain | Residue |
| A | ALA2 |
| A | ASP4 |
| A | ASN6 |
| A | ASP42 |
| A | ASP96 |
| A | HOH1003 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 702 |
| Chain | Residue |
| A | ASP151 |
| A | GLY187 |
| A | ASP189 |
| A | HOH826 |
| A | ASN145 |
| A | ASP147 |
| A | ASN150 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 703 |
| Chain | Residue |
| A | ASP276 |
| A | ASN279 |
| A | PHE281 |
| A | SER283 |
| A | GLU288 |
| A | HOH1369 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MPD A 704 |
| Chain | Residue |
| A | HIS221 |
| A | TYR223 |
| A | PHE313 |
| A | HOH945 |
| A | HOH1061 |
| A | HOH1377 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 701 |
| Chain | Residue |
| B | ALA2 |
| B | ASP4 |
| B | ASN6 |
| B | ASP42 |
| B | ASP96 |
| B | HOH935 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 702 |
| Chain | Residue |
| B | ASN145 |
| B | ASP147 |
| B | ASN150 |
| B | ASP151 |
| B | GLY187 |
| B | ASP189 |
| B | HOH833 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 703 |
| Chain | Residue |
| B | ASP276 |
| B | ASN279 |
| B | PHE281 |
| B | SER283 |
| B | GLU288 |
| B | HOH1460 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 704 |
| Chain | Residue |
| B | HIS221 |
| B | TYR223 |
| B | PHE313 |
| B | HOH839 |
| B | HOH877 |
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 | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12051850","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JI1","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 |
