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NMR structure of cbp bromodomain in complex with P53 peptide

Analyse NMR structure of cbp bromodomain in complex with P53 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JSP
Type: protein
Length: 141 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor protein P53; Creb-binding protein
UniProt: P04637, Q92793

Structure

solution nmr · 2 distinct chains · 36% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tumor protein P53	protein	20	0% helix, 0% strand	P04637
B	Creb-binding protein	protein	121	42% helix, 2% strand	Q92793

Interfaces

1 interface between chains.

A–B · 412 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

1JSP · NMR Structure of CBP Bromodomain in complex with p53 peptide · 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 B against A, TM-score 0.70

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 P04637
Every structure of UniProt Q92793
Elsewhere: RCSB PDB 1JSP · PDBe 1JSP · UniProt P04637 · UniProt Q92793

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