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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
DetailsModified residue: {"description":"Phosphoserine; by LATS1 and LATS2","evidences":[{"source":"PubMed","id":"17974916","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18158288","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-lactoyllysine","evidences":[{"source":"PubMed","id":"38512451","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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