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Solution structure of the kix domain of cbp bound to the transactivation domain of C-myb

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

PDB: 1SB0
Type: protein
Length: 112 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein cbp; Protein C-myb
UniProt: P45481, P06876

Structure

solution nmr · 2 distinct chains · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein cbp	protein	87	71% helix, 0% strand	P45481
B	Protein C-myb	protein	25	80% helix, 0% strand	P06876

Interfaces

1 interface between chains.

A–B · 691 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1SB0 · Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb · 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 0.80
P06876 · AlphaFold monomer V2.0 prediction for transcriptional activator myb (P06876) · a predicted model of the same protein · chain B against A, TM-score 0.35

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 P06876
Elsewhere: RCSB PDB 1SB0 · PDBe 1SB0 · UniProt P45481 · UniProt P06876

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