6VOY
Cryo-EM structure of HTLV-1 instasome
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004521 | molecular_function | RNA endonuclease activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015074 | biological_process | DNA integration |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0004521 | molecular_function | RNA endonuclease activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015074 | biological_process | DNA integration |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0004521 | molecular_function | RNA endonuclease activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0015074 | biological_process | DNA integration |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0004521 | molecular_function | RNA endonuclease activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0015074 | biological_process | DNA integration |
| E | 0000159 | cellular_component | protein phosphatase type 2A complex |
| E | 0007165 | biological_process | signal transduction |
| E | 0019888 | molecular_function | protein phosphatase regulator activity |
| F | 0000159 | cellular_component | protein phosphatase type 2A complex |
| F | 0007165 | biological_process | signal transduction |
| F | 0019888 | molecular_function | protein phosphatase regulator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS6 |
| A | HIS10 |
| A | CYS33 |
| A | CYS36 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | ASP63 |
| A | ASP120 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | CYS33 |
| B | CYS36 |
| B | HIS6 |
| B | HIS10 |
| B | SER32 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | HIS6 |
| C | HIS10 |
| C | CYS33 |
| C | CYS36 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue MG C 302 |
| Chain | Residue |
| C | ASP63 |
| I | DG24 |
| N | DG18 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | HIS6 |
| D | HIS10 |
| D | CYS33 |
| D | CYS36 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:3132977, ECO:0000269|PubMed:9720912 |
| Chain | Residue | Details |
| A | LYS-70 | |
| B | LYS-11 | |
| C | LYS-70 | |
| C | LYS-68 | |
| C | LYS-14 | |
| C | LYS-12 | |
| C | LYS-11 | |
| D | LYS-70 | |
| D | LYS-68 | |
| D | LYS-14 | |
| D | LYS-12 | |
| A | LYS-68 | |
| D | LYS-11 | |
| A | LYS-14 | |
| A | LYS-12 | |
| A | LYS-11 | |
| B | LYS-70 | |
| B | LYS-68 | |
| B | LYS-14 | |
| B | LYS-12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 200 |
| Details | DNA_BIND: Integrase-type => ECO:0000255|PROSITE-ProRule:PRU00506 |
| Chain | Residue | Details |
| A | HIS226-CYS276 | |
| B | HIS226-CYS276 | |
| C | HIS226-CYS276 | |
| D | HIS226-CYS276 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00457 |
| Chain | Residue | Details |
| A | ASP63 | |
| A | ASP120 | |
| B | ASP63 | |
| B | ASP120 | |
| C | ASP63 | |
| C | ASP120 | |
| D | ASP63 | |
| D | ASP120 |
