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NMR structure of the complex between the kix domain of cbp and the transactivation domain 1 of P65

Analyse NMR structure of the complex between the kix domain of cbp and the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5U4K
Type: protein
Length: 120 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Creb-binding protein; Transcription factor P65
UniProt: A0A0U1RPQ3, Q04206
Pockets: 1 · best druggability 0.50

Structure

solution nmr · 2 distinct chains · 59% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Creb-binding protein	protein	87	71% helix, 0% strand	A0A0U1RPQ3
B	Transcription factor P65	protein	33	27% helix, 0% strand	Q04206

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	51	0.50	0.87	15	empty

Interfaces

1 interface between chains.

A–B · 727 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5U4K · NMR structure of the complex between the KIX domain of CBP and the transactivation domain… · the same entry in another collection · chain A against A, TM-score 1.00
Q04206 · AlphaFold monomer V2.0 prediction for transcription factor P65 (Q04206) · a predicted model of the same protein · chain B against A, TM-score 0.41

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 A0A0U1RPQ3
Every structure of UniProt Q04206
Elsewhere: RCSB PDB 5U4K · PDBe 5U4K · UniProt A0A0U1RPQ3 · UniProt Q04206

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