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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

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A
(A)
Transcriptional enhancer factor TEF-3polymer21925426.71UniProt (Q15561)
Pfam (PF17725)
Homo sapiens (Human)TEA domain family member 4,TEAD-4,Transcription factor 13-like 1,Transcription factor RTEF-1
2B
(L)
Transcriptional coactivator YAP1polymer414650.31UniProt (P46937)
Pfam (PF15238)
Homo sapiens (Human)Yes-associated protein 1,Protein yorkie homolog,Yes-associated protein YAP65 homolog
3C
(A)
MYRISTIC ACIDnon-polymer228.41Chemie (MYR)
4D, E, F, G
(A)
PHOSPHATE IONnon-polymer95.04Chemie (PO4)
5H, I
(A, L)
waterwater18.0197Chemie (HOH)
Sequence modifications
A: 216 - 434 (UniProt: Q15561)
PDBExternal DatabaseDetails
Ala 263Glu 220engineered mutation
Phe 429Tyr 386engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains2
Total formula weight30077.0
Non-Polymers*Number of molecules5
Total formula weight608.3
All*Total formula weight30685.3
*Water molecules are not included.

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PDB entries from 2025-07-23

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