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GENERAL
TITLE
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
DATE LAST MODIFIED
31 Oct 2018
RELEASE
19 Sept 2018
OBSOLETE
CLASSIFICATION
TRANSCRIPTION
EXPERIMENT TYPE
X-RAY DIFFRACTION
SPACE GROUP
P 41 21 2
RESOLUTION RANGE HIGH
1.85
RESOLUTION RANGE LOW
19.96
PUBMED ID
DOI
10.1002/PRO.3493
LIGANDS

Chains

Structure ChainTarget ProteinGeneExpression SystemOrganismSynonimsActions
Q15561 TEAD4, RTEF1, TCF13L1, TEF3 ESCHERICHIA COLI HUMAN
TEA DOMAIN FAMILY MEMBER 4,TEAD-4,TRANSCRIPTION FA ...
Mutations
P46937 -- -- HUMAN
YES-ASSOCIATED PROTEIN 1,PROTEIN YORKIE HOMOLOG,YE ...
Mutations
NGL Viewer is used for the molecular visualization.
  • AS Rose, AR Bradley, Y Valasatava, JM Duarte, A Prlić and PW Rose. NGL viewer: web-based molecular graphics for large complexes. Bioinformatics: bty419, 2018. doi:10.1093/bioinformatics/bty419
  • AS Rose and PW Hildebrand. NGL Viewer: a web application for molecular visualization. Nucl Acids Res (1 July 2015) 43 (W1): W576-W579 first published online April 29, 2015. doi:10.1093/nar/gkv402