1NLW: Mad-Max recognizing DNA

Crystal structure of Mad-Max recognizing DNA. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 Feb 2003.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 8
Atoms: 4,212
Mol. weight: 59.2 kDa
Released: 4 Feb 2003

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

Secondary structure: helices and β-sheets

1NLW contains 8 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: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-26	24
α-helix	40-79	40

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	204-226	23
α-helix	239-277	39

Chain D: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	503-526	24
α-helix	539-577	39

Chain E: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	706-726	21
α-helix	739-777	39

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
5'-d(gpapgptpapgpcpapcpgptpgpcptpapcptpc)-3'	F, G, H, J	DNA	18
Mad protein	A, D	protein	80	Homo sapiens	Q05195 (AlphaFold model)
Max protein	B, E	protein	76	Homo sapiens	P61244 (AlphaFold model)

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

>1NLW_1 5'-D(*GP*AP*GP*TP*AP*GP*CP*AP*CP*GP*TP*GP*CP*TP*AP*CP*TP*C)-3' (chains F, G, H, J)
GAGTAGCACGTGCTACTC

Sequence of entity 2 (A, D), FASTA

>1NLW_2 MAD PROTEIN (chains A, D)
SRSTHNEMEKNRRAHLRLSLEKLKGLVPLGPDSSRHTTLSLLTKAKLHIKKLEDSDRKAV
HQIDQLQREQRHLKRQLEKL

Sequence of entity 3 (B, E), FASTA

>1NLW_3 MAX PROTEIN (chains B, E)
KRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQ
DIDDLKRQNALLEQQV

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 Q05195 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1E91 Structure of the complex of the Mad1-Sin3B interaction domains
1G1E NMR structure of the human MAD1 transrepression domain sid in complex with mammalian…
1PD7 Extended SID of Mad1 bound to the PAH2 domain of mSin3B
1S5Q Solution Structure of Mad1 SID-mSin3A PAH2 Complex

Browse structure collections

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