1U2R
Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003746 | molecular_function | translation elongation factor activity |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006414 | biological_process | translational elongation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019843 | molecular_function | rRNA binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043022 | molecular_function | ribosome binding |
| A | 0045901 | biological_process | positive regulation of translational elongation |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| A | 1990145 | biological_process | maintenance of translational fidelity |
| A | 1990904 | cellular_component | ribonucleoprotein complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 843 |
| Chain | Residue |
| A | SER33 |
| A | GDP1920 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE APR A 1699 |
| Chain | Residue |
| A | VAL306 |
| A | HIS694 |
| A | ASP696 |
| A | ILE698 |
| A | DDE699 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SO1 A 1700 |
| Chain | Residue |
| A | TYR521 |
| A | SER523 |
| A | GLU524 |
| A | VAL561 |
| A | ALA562 |
| A | PRO727 |
| A | PHE729 |
| A | MET796 |
| A | VAL797 |
| A | PHE798 |
| A | TRP801 |
| A | HOH1921 |
| A | HOH1940 |
| A | HOH1951 |
| A | GLN490 |
| A | LEU519 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP A 1920 |
| Chain | Residue |
| A | HIS27 |
| A | ASP29 |
| A | HIS30 |
| A | GLY31 |
| A | LYS32 |
| A | SER33 |
| A | THR34 |
| A | ASN158 |
| A | LYS159 |
| A | ASP161 |
| A | ARG162 |
| A | SER213 |
| A | GLY214 |
| A | LEU215 |
| A | MG843 |
| A | HOH1939 |
| A | HOH1988 |
| A | HOH2031 |
| A | HOH2035 |
Functional Information from PROSITE/UniProt
| site_id | PS00301 |
| Number of Residues | 16 |
| Details | G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DTrkdEQeRGITIksT |
| Chain | Residue | Details |
| A | ASP58-THR73 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17082187","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1U2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NPF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17082187","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1U2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NPF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine; by EFM3; alternate","evidences":[{"source":"PubMed","id":"24517342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25086354","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine; by EFM2; alternate","evidences":[{"source":"PubMed","id":"24517342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25086354","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Diphthamide","evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16950777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"721806","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | ASP29 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | HIS108 |
