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Structure of cbp nuclear coactivator binding domain in complex with P53 tad

Analyse Structure of cbp nuclear coactivator binding domain in complex with P53 tad in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2L14
Type: protein
Length: 108 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Creb-binding protein; Cellular tumor antigen P53
UniProt: P45481, P04637
Pockets: 1 · best druggability 0.61

Structure

solution nmr · 2 distinct chains · 49% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Creb-binding protein	protein	59	58% helix, 0% strand	P45481
B	Cellular tumor antigen P53	protein	49	39% helix, 0% strand	P04637

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	107	0.61	0.86	22	empty

Interfaces

1 interface between chains.

A–B · 1152 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

2L14 · Structure of CBP nuclear coactivator binding domain in complex with p53 TAD · 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 0.47

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
Every structure of UniProt P04637
Elsewhere: RCSB PDB 2L14 · PDBe 2L14 · UniProt P45481 · UniProt P04637

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