6GE6
X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(wildtype): The role of residual flexibility and water molecules in the adaptation of a bound intrinsically disordered protein to mutations at a binding interface
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MYR A 501 |
| Chain | Residue |
| A | VAL334 |
| A | LYS344 |
| A | CYS367 |
| A | ILE395 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue PO4 A 502 |
| Chain | Residue |
| A | SER253 |
| A | SER254 |
| A | HIS426 |
| A | HOH617 |
| A | HOH654 |
| A | HOH661 |
| A | HOH705 |
| A | GLY216 |
| A | HIS249 |
| A | ILE250 |
| A | GLY251 |
| A | GLN252 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 503 |
| Chain | Residue |
| A | ARG351 |
| A | ARG351 |
| A | SER358 |
| A | ARG360 |
| A | HOH623 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue PO4 A 504 |
| Chain | Residue |
| A | GLU228 |
| A | LYS244 |
| A | SER317 |
| A | HIS362 |
| A | HIS362 |
| A | HOH627 |
| A | HOH628 |
| A | HOH642 |
| A | HOH655 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 505 |
| Chain | Residue |
| A | GLN319 |
| A | ARG360 |
| A | HIS362 |
| A | ARG363 |
| A | HOH628 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by LATS1 and LATS2 => ECO:0000269|PubMed:17974916, ECO:0000269|PubMed:18158288, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| L | SER61 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| L | THR63 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-lactoyllysine => ECO:0000269|PubMed:38512451 |
| Chain | Residue | Details |
| L | LYS90 |
