Research workbench

AML1/CBFBETA complex

Analyse AML1/CBFBETA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1E50
Type: protein
Length: 1,208 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Core-binding factor alpha subunit; Core-binding factor cbf-beta
UniProt: Q01196, Q13951
Pockets: 13 · best druggability 0.48

Structure

x-ray diffraction · 6 distinct chains · 9% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Core-binding factor alpha subunit	protein	115	0% helix, 47% strand	Q01196
B, H	Core-binding factor cbf-beta	protein	130	23% helix, 35% strand	Q13951
C	Core-binding factor alpha subunit	protein	125	0% helix, 43% strand	Q01196
D, F	Core-binding factor cbf-beta	protein	125	26% helix, 41% strand	Q13951
E, G	Core-binding factor alpha subunit	protein	119	0% helix, 45% strand	Q01196
Q, R	Core-binding factor alpha subunit	protein	110	0% helix, 43% strand	Q01196

Pockets

13 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	181	0.48	0.76	21	empty
2	180	0.47	0.76	25	empty
3	181	0.47	0.76	26	empty
4	161	0.42	0.74	24	empty
5	120	0.40	0.75	13	empty

Interfaces

14 interfaces between chains.

A–B · 1180 Å² buried · 18 hydrogen bonds · protein-protein
G–H · 1134 Å² buried · 19 hydrogen bonds · protein-protein
E–F · 1029 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 1023 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 672 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1E50 · AML1/CBFbeta complex · the same entry in another collection · chain R against R, TM-score 1.00
Q13951 · AlphaFold monomer V2.0 prediction for core-binding factor subunit beta (Q13951) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q01196
Every structure of UniProt Q13951
Elsewhere: RCSB PDB 1E50 · PDBe 1E50 · UniProt Q01196 · UniProt Q13951

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