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The crystal structures of human MYC:MAX bhlhzip complex

Analyse The crystal structures of human MYC:MAX bhlhzip complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6G6L
Type: protein
Length: 589 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myc proto-oncogene protein; Protein max
UniProt: P01106, P61244
Ligands: SO4
Pockets: 8 · best druggability 0.38

Structure

x-ray diffraction · 6 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E	Myc proto-oncogene protein	protein	78	78% helix, 0% strand	P01106
B	Protein max	protein	68	82% helix, 0% strand	P61244
C	Myc proto-oncogene protein	protein	79	80% helix, 0% strand	P01106
D, F	Protein max	protein	71	85% helix, 0% strand	P61244
G	Myc proto-oncogene protein	protein	77	78% helix, 0% strand	P01106
H	Protein max	protein	67	84% helix, 0% strand	P61244

Ligands and binding sites

SO4 · Sulfate ion · ion · 14 copies · chains A, B, G, C, D, E, F, H

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 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	81	0.38	0.77	18	empty
2	121	0.38	0.73	17	empty
3	103	0.37	0.74	18	empty
4	103	0.37	0.74	12	empty
5	60	0.35	0.78	17	empty

Interfaces

12 interfaces between chains.

C–D · 1768 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 1733 Å² buried · 15 hydrogen bonds · protein-protein
G–H · 1720 Å² buried · 17 hydrogen bonds · protein-protein
E–F · 1708 Å² buried · 15 hydrogen bonds · protein-protein
E–H · 400 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6G6L · The crystal structures of Human MYC:MAX bHLHZip complex · the same entry in another collection · chain H against H, TM-score 1.00
P61244 · AlphaFold monomer V2.0 prediction for protein max (P61244) · a predicted model of the same protein · chain B against A, TM-score 0.97
P01106 · AlphaFold monomer V2.0 prediction for myc proto-oncogene protein (P01106) · a predicted model of the same protein · chain C against A, TM-score 0.96

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 P01106
Every structure of UniProt P61244
Elsewhere: RCSB PDB 6G6L · PDBe 6G6L · UniProt P01106 · UniProt P61244

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