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NMR structure of P/CAF bromodomain in complex with HIV-1 tat peptide

Analyse NMR structure of P/CAF bromodomain in complex with HIV-1 tat peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JM4
Type: protein
Length: 129 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 tat peptide; P300/CBP-associated factor
UniProt: Q92831
Pockets: 1 · best druggability 0.33

Structure

solution nmr · 2 distinct chains · 51% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HIV-1 tat peptide	protein	11	0% helix, 0% strand	—
B	P300/CBP-associated factor	protein	118	56% helix, 2% strand	Q92831

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	62	0.33	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 610 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

1JM4 · NMR Structure of P/CAF Bromodomain in Complex with HIV-1 Tat Peptide · the same entry in another collection · chain A against A, TM-score 1.00
Q92831 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT2B (Q92831) · a predicted model of the same protein · chain B against A, TM-score 0.76

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 Q92831
Elsewhere: RCSB PDB 1JM4 · PDBe 1JM4 · UniProt Q92831

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