6G6L: Human MYC:MAX bHLHZip complex

The crystal structures of Human MYC:MAX bHLHZip complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Apr 2019.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 8
Atoms: 5,511
Mol. weight: 86.99 kDa
Released: 10 Apr 2019

Explore 6G6L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6G6L contains 20 α-helices and 0 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and E: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	909-925	17
α-helix	939-982	44

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	215-227	13
α-helix	230-232	3
α-helix	239-278	40

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	907-925	19
α-helix	939-982	44

Chain D: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	212-228	17
α-helix	230-232	3
α-helix	239-278	40

Chain F: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	212-227	16
α-helix	230-232	3
α-helix	239-278	40

Chain G: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	910-925	16
α-helix	939-982	44

Chain H: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	216-228	13
α-helix	230-232	3
α-helix	239-278	40

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myc proto-oncogene protein	A, C, E, G	protein	94	Homo sapiens	P01106 (AlphaFold model)
Protein max	B, D, F, H	protein	83	Homo sapiens	P61244 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>6G6L_1 Myc proto-oncogene protein (chains A, C, E, G)
MHHHHHHEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYI
LSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNS

Sequence of entity 2 (B, D, F, H), FASTA

>6G6L_2 Protein max (chains B, D, F, H)
MADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHT
HQQDIDDLKRQNALLEQQVRALE

Primary citation

Crystal Structures and Nuclear Magnetic Resonance Studies of the Apo Form of the c-MYC:MAX bHLHZip Complex Reveal a Helical Basic Region in the Absence of DNA. Sammak, S., Hamdani, N., Gorrec, F. et al. Biochemistry (2019) 58:3144-3154. DOI 10.1021/acs.biochem.9b00296 · PubMed

Other PDB entries of the same protein (UniProt P01106 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9QNH 1.3 Å, Myc pS294 phosphopeptide binding to 14-3-3sigma
6G6K 1.35 Å, The crystal structures of Human MYC:MAX bHLHZip complex
1NKP 1.8 Å, Crystal structure of Myc-Max recognizing DNA
8Q1N 1.84 Å, Cyclic peptide binder of the WBM-site of WDR5
4Y7R 1.9 Å, Crystal structure of WDR5 in complex with MYC MbIIIb peptide
8J2Q 1.92 Å, Crystal structure of Cypovirus Polyhedra mutant fused with c-Myc fragment
5I4Z 1.95 Å, Structure of apo OmoMYC
8X8V 2.0 Å, Crystal structure of Cypovirus Polyhedra mutant fused with c-Myc fragment
8X8S 2.04 Å, Crystal structure of Cypovirus Polyhedra mutant fused with c-Myc fragment
1EE4 2.1 Å, Crystal structure of yeast karyopherin (importin) alpha in a complex with a C-myc nls…
6G6J 2.25 Å, The crystal structures of Human MYC:MAX bHLHZip complex
6E16 2.4 Å, Ternary structure of c-Myc-TBP-TAF1

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