4X33
Structure of the Elongator cofactor complex Kti11/Kti13 at 1.45A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0017183 | biological_process | protein histidyl modification to diphthamide |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0002098 | biological_process | tRNA wobble uridine modification |
| B | 0003674 | molecular_function | molecular_function |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| B | 0008033 | biological_process | tRNA processing |
| B | 0016567 | biological_process | protein ubiquitination |
| B | 0017183 | biological_process | protein histidyl modification to diphthamide |
| B | 0061630 | molecular_function | ubiquitin protein ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue FE A 101 |
| Chain | Residue |
| A | CYS25 |
| A | CYS27 |
| A | CYS47 |
| A | CYS50 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 102 |
| Chain | Residue |
| A | TYR4 |
| A | MET53 |
| A | HOH245 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 103 |
| Chain | Residue |
| A | PHE14 |
| A | HOH211 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 104 |
| Chain | Residue |
| A | HOH230 |
| B | GLN139 |
| B | HOH903 |
| B | HOH905 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 401 |
| Chain | Residue |
| B | ILE37 |
| B | ASN53 |
| B | ASP54 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 402 |
| Chain | Residue |
| B | LEU312 |
| B | HOH667 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 403 |
| Chain | Residue |
| B | THR119 |
| B | GLN120 |
| B | HOH589 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 404 |
| Chain | Residue |
| B | PRO302 |
| B | LYS304 |
| B | HOH622 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 405 |
| Chain | Residue |
| B | ASP260 |
| B | PHE261 |
| B | HOH863 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue DXE B 406 |
| Chain | Residue |
| B | ARG13 |
| B | GLY18 |
| B | HIS19 |
| B | ASP20 |
| B | ARG64 |
| B | ARG75 |
| B | HOH584 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 407 |
| Chain | Residue |
| B | HOH529 |
| B | HOH568 |
| B | HOH617 |
| B | HOH647 |
| B | HOH658 |
| B | HOH672 |
Functional Information from PROSITE/UniProt
| site_id | PS00626 |
| Number of Residues | 11 |
| Details | RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IACGgNHSVML |
| Chain | Residue | Details |
| B | ILE41-LEU51 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25543256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25604895","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4D4O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D4P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X33","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 49 |
| Details | Repeat: {"description":"RCC1 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 51 |
| Details | Repeat: {"description":"RCC1 3"} |
| Chain | Residue | Details |
