6GE3
X-ray structure of TEAD4 (wildtype) 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 | 8 |
Details | binding site for residue MYR A 501 |
Chain | Residue |
A | PHE229 |
A | ALA231 |
A | LYS344 |
A | LEU366 |
A | CYS367 |
A | MET370 |
A | LEU390 |
A | ILE395 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | LYS273 |
A | PHE337 |
A | GLY338 |
A | ASN392 |
A | HOH601 |
A | HOH718 |
L | GLN82 |
L | THR83 |
L | ARG89 |
A | ASP272 |
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 |