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NMR structure of FOXO3A transactivation domains (CR2C-CR3) in complex with cbp kix domain (2B3L conformation)

Analyse NMR structure of FOXO3A transactivation domains (CR2C-CR3) in complex with cbp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LQH
Type: protein
Length: 139 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Creb-binding protein; Forkhead box O3
EC: 2.3.1.48
UniProt: P45481
Pockets: 1 · best druggability 0.35

Structure

solution nmr · 2 distinct chains · 68% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Creb-binding protein (EC 2.3.1.48)	protein	87	82% helix, 0% strand	P45481
B	Forkhead box O3	protein	52	44% helix, 0% strand	—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	102	0.35	0.74	23	empty

Interfaces

1 interface between chains.

A–B · 1577 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

2LQH · NMR structure of FOXO3a transactivation domains (CR2C-CR3) in complex with CBP KIX domain… · the same entry in another collection · chain A against A, TM-score 1.00
P45481 · AlphaFold monomer V2.0 prediction for histone lysine acetyltransferase crebbp (P45481) · a predicted model of the same protein · chain A against A, TM-score 0.79

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 P45481
Elsewhere: RCSB PDB 2LQH · PDBe 2LQH · UniProt P45481

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