1NKP: Myc-Max recognizing DNA

Crystal structure of Myc-Max recognizing DNA. Determined by X-ray diffraction at 1.8 Å resolution. Released 4 Feb 2003.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 8
Atoms: 4,906
Mol. weight: 63.75 kDa
Released: 4 Feb 2003

Explore 1NKP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1NKP contains 12 α-helices and 0 β-strands across 4 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.

Chain A: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	898-925	28
α-helix	929-931	3
α-helix	939-981	43

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	203-226	24
α-helix	230-232	3
α-helix	239-279	41

Chain D: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	500-525	26
α-helix	529-531	3
α-helix	539-580	42

Chain E: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	705-726	22
α-helix	730-732	3
α-helix	739-779	41

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
5'-d(cpgpapgptpapgpcpapcpgptpgpcptpapcptp*c)-3'	F, G, H, J	DNA	19
Myc proto-oncogene protein	A, D	protein	88	Homo sapiens	P01106 (AlphaFold model)
Max protein	B, E	protein	83	Homo sapiens	P61244 (AlphaFold model)

Sequence of entity 1 (F, G, H, J), FASTA

>1NKP_1 5'-D(*CP*GP*AP*GP*TP*AP*GP*CP*AP*CP*GP*TP*GP*CP*TP*AP*CP*TP*C)-3' (chains F, G, H, J)
CGAGTAGCACGTGCTACTC

Sequence of entity 2 (A, D), FASTA

>1NKP_2 Myc proto-oncogene protein (chains A, D)
GHMNVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAE
EQKLISEEDLLRKRREQLKHKLEQLGGC

Sequence of entity 3 (B, E), FASTA

>1NKP_3 Max protein (chains B, E)
DKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQ
QDIDDLKRQNALLEQQVRALGGC

Primary citation

X-ray structures of Myc-Max and Mad-Max recognizing DNA: Molecular bases of regulation by proto-oncogenic transcription factors. Nair, S.K., Burley, S.K. Cell (2003) 112:193-205. DOI 10.1016/S0092-8674(02)01284-9 · 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
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…
6G6L 2.2 Å, The crystal structures of Human MYC:MAX bHLHZip complex
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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