6HB4
TFAM in Complex with Site-Y
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | THR150 |
| A | LYS154 |
| A | LYS156 |
| C | DT7 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | GLU214 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue 1PE A 303 |
| Chain | Residue |
| F | DC4 |
| F | DA5 |
| A | HIS137 |
| A | LEU138 |
| A | LYS141 |
| E | DA22 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue 1PE A 304 |
| Chain | Residue |
| A | LYS118 |
| A | GLU130 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue 1PE D 301 |
| Chain | Residue |
| D | ILE114 |
| D | LYS118 |
| D | ILE126 |
| D | LEU129 |
| D | GLU130 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue 1PE G 301 |
| Chain | Residue |
| G | LYS118 |
| G | ILE126 |
| G | GLU130 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 272 |
| Details | DNA_BIND: HMG box 1 => ECO:0000255|PROSITE-ProRule:PRU00267 |
| Chain | Residue | Details |
| A | PRO50-LYS118 | |
| D | PRO50-LYS118 | |
| G | PRO50-LYS118 | |
| J | PRO50-LYS118 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 256 |
| Details | DNA_BIND: HMG box 2 => ECO:0000255|PROSITE-ProRule:PRU00267 |
| Chain | Residue | Details |
| A | PRO155-GLU219 | |
| D | PRO155-GLU219 | |
| G | PRO155-GLU219 | |
| J | PRO155-GLU219 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | SITE: Intercalates between bases and promotes DNA bending |
| Chain | Residue | Details |
| A | LEU58 | |
| A | LEU182 | |
| D | LEU58 | |
| D | LEU182 | |
| G | LEU58 | |
| G | LEU182 | |
| J | LEU58 | |
| J | LEU182 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:23201127 |
| Chain | Residue | Details |
| A | SER55 | |
| G | SER56 | |
| G | SER61 | |
| G | SER160 | |
| J | SER55 | |
| J | SER56 | |
| J | SER61 | |
| J | SER160 | |
| A | SER56 | |
| A | SER61 | |
| A | SER160 | |
| D | SER55 | |
| D | SER56 | |
| D | SER61 | |
| D | SER160 | |
| G | SER55 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR122 | |
| D | THR122 | |
| G | THR122 | |
| J | THR122 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER193 | |
| D | SER193 | |
| G | SER193 | |
| J | SER193 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER195 | |
| D | SER195 | |
| G | SER195 | |
| J | SER195 |
