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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_idAC1
Number of Residues4
Detailsbinding site for residue MYR A 501
ChainResidue
AVAL334
ALYS344
ACYS367
AILE395

site_idAC2
Number of Residues12
Detailsbinding site for residue PO4 A 502
ChainResidue
ASER253
ASER254
AHIS426
AHOH617
AHOH654
AHOH661
AHOH705
AGLY216
AHIS249
AILE250
AGLY251
AGLN252

site_idAC3
Number of Residues5
Detailsbinding site for residue PO4 A 503
ChainResidue
AARG351
AARG351
ASER358
AARG360
AHOH623

site_idAC4
Number of Residues9
Detailsbinding site for residue PO4 A 504
ChainResidue
AGLU228
ALYS244
ASER317
AHIS362
AHIS362
AHOH627
AHOH628
AHOH642
AHOH655

site_idAC5
Number of Residues5
Detailsbinding site for residue PO4 A 505
ChainResidue
AGLN319
AARG360
AHIS362
AARG363
AHOH628

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

239149

PDB entries from 2025-07-23

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