3WBM
Crystal Structure of protein-RNA complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003690 | molecular_function | double-stranded DNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0005694 | cellular_component | chromosome |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0030261 | biological_process | chromosome condensation |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003690 | molecular_function | double-stranded DNA binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0005694 | cellular_component | chromosome |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0030261 | biological_process | chromosome condensation |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003690 | molecular_function | double-stranded DNA binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0004518 | molecular_function | nuclease activity |
| C | 0005694 | cellular_component | chromosome |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0030261 | biological_process | chromosome condensation |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003690 | molecular_function | double-stranded DNA binding |
| D | 0003723 | molecular_function | RNA binding |
| D | 0004518 | molecular_function | nuclease activity |
| D | 0005694 | cellular_component | chromosome |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0030261 | biological_process | chromosome condensation |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24307170, ECO:0007744|PDB:3WBM |
| Chain | Residue | Details |
| A | LYS16 | |
| B | ARG44 | |
| C | LYS16 | |
| C | LYS17 | |
| C | TYR22 | |
| C | ARG42 | |
| C | ARG44 | |
| D | LYS16 | |
| D | LYS17 | |
| D | TYR22 | |
| D | ARG42 | |
| A | LYS17 | |
| D | ARG44 | |
| A | TYR22 | |
| A | ARG42 | |
| A | ARG44 | |
| B | LYS16 | |
| B | LYS17 | |
| B | TYR22 | |
| B | ARG42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P60849 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 | |
| C | SER2 | |
| D | SER2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-methylated lysine; alternate => ECO:0000250|UniProtKB:F0NHH1 |
| Chain | Residue | Details |
| A | LYS16 | |
| B | LYS16 | |
| C | LYS16 | |
| D | LYS16 |
