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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_idAC1
Number of Residues8
Detailsbinding site for residue MYR A 501
ChainResidue
APHE229
AALA231
ALYS344
ALEU366
ACYS367
AMET370
ALEU390
AILE395

site_idAC2
Number of Residues10
Detailsbinding site for residue GOL A 502
ChainResidue
ALYS273
APHE337
AGLY338
AASN392
AHOH601
AHOH718
LGLN82
LTHR83
LARG89
AASP272

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_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
ChainResidueDetails
LSER61

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
LTHR63

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PDB entries from 2024-05-01

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