1TQP
Crystal Structure of A. fulgidus Rio2 Serine Protein Kinase Bound to ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030490 | biological_process | maturation of SSU-rRNA |
| A | 0030688 | cellular_component | preribosome, small subunit precursor |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP A 283 |
| Chain | Residue |
| A | MSE98 |
| A | ILE182 |
| A | GLU186 |
| A | TYR222 |
| A | ASN223 |
| A | ILE234 |
| A | ASP235 |
| A | HOH285 |
| A | HOH307 |
| A | HOH367 |
| A | HOH402 |
| A | GLY101 |
| A | HOH409 |
| A | LYS102 |
| A | GLU103 |
| A | SER104 |
| A | LYS120 |
| A | PRO167 |
| A | MSE179 |
| A | GLU180 |
Functional Information from PROSITE/UniProt
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. IVHgDLSQYNVLV |
| Chain | Residue | Details |
| A | ILE214-VAL226 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15943813","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15943813","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZAO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15341724","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15943813","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZAO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15341724","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TQP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"15943813","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2phk |
| Chain | Residue | Details |
| A | ASP218 | |
| A | SER220 |
