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Crystal structure of PHD finger-linker-bromodomain fragment of human BPTF in the free form External Resource: Annotation Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) A SCOP2B Superfamily Bromodomain 8084225 3001843 SCOP2B (2022-06-29) A SCOP2B Superfamily FYVE/PHD zinc finger 8067574 3001459 SCOP2B (2022-06-29) B SCOP2B Superfamily Bromodomain 8084225 3001843 SCOP2B (2022-06-29) B SCOP2B Superfamily FYVE/PHD zinc finger 8067574 3001459 SCOP2B (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A Bromodomain e2f6nA1 A: alpha bundles X: Bromodomain-like H: Bromodomain (From Topology) T: Bromodomain F: Bromodomain ECOD (1.6) A PHD e2f6nA2 A: few secondary structure elements X: RING/U-box-like H: RING/U-box-like T: FYVE/PHD zinc finger F: PHD ECOD (1.6) B Bromodomain e2f6nB1 A: alpha bundles X: Bromodomain-like H: Bromodomain (From Topology) T: Bromodomain F: Bromodomain ECOD (1.6) B PHD e2f6nB2 A: few secondary structure elements X: RING/U-box-like H: RING/U-box-like T: FYVE/PHD zinc finger F: PHD ECOD (1.6)
Chains Accession Name Description Comments Source PF00439 Bromodomain (Bromodomain) Bromodomain Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine [3]. Domain PF00628 PHD-finger (PHD) PHD-finger PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3]. Domain
Chains Polymer Molecular Function Biological Process Cellular Component bromodomain PHD finger transcription factor
Chains Drug Target   Associated Disease Pharos :  Q12830