1QWO
Crystal structure of a phosphorylated phytase from Aspergillus fumigatus, revealing the structural basis for its heat resilience and catalytic pathway
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016791 | molecular_function | phosphatase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00616 |
| Number of Residues | 15 |
| Details | HIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. ItlVqvLsRHGaRyP |
| Chain | Residue | Details |
| A | ILE50-PRO64 |
| site_id | PS00778 |
| Number of Residues | 17 |
| Details | HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. MyVDfSHDNSMvsIffA |
| Chain | Residue | Details |
| A | MET332-ALA348 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15136045","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QWO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15341723","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1SK8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15341723","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1SK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SK9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P34752","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15136045","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15341723","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QWO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SKB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15136045","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15341723","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QWO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SK9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SKA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SKB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15136045","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QWO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rpt |
| Chain | Residue | Details |
| A | HIS338 | |
| A | ARG142 | |
| A | ASP339 | |
| A | ARG62 |
