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The structure of E-protein activation domain 1 bound to the kix domain of CBP/P300 elucidates leukemia induction by E2A-PBX1

Analyse The structure of E-protein activation domain 1 bound to the kix domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KWF
Type: protein
Length: 106 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Creb-binding protein; Transcription factor 4
EC: 2.3.1.48
UniProt: Q92793, P15884

Structure

solution nmr · 2 distinct chains · 64% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Creb-binding protein (EC 2.3.1.48)	protein	87	66% helix, 0% strand	Q92793
B	Transcription factor 4	protein	19	58% helix, 0% strand	P15884

Interfaces

1 interface between chains.

A–B · 777 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

2KWF · The structure of E-protein activation domain 1 bound to the KIX domain of CBP/p300… · the same entry in another collection · chain A against A, TM-score 1.00
Q92793 · AlphaFold monomer V2.0 prediction for creb-binding protein (Q92793) · a predicted model of the same protein · chain A against A, TM-score 0.78
P15884 · AlphaFold monomer V2.0 prediction for transcription factor 4 (P15884) · a predicted model of the same protein · chain B against A, TM-score 0.42

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q92793
Every structure of UniProt P15884
Elsewhere: RCSB PDB 2KWF · PDBe 2KWF · UniProt Q92793 · UniProt P15884

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