1MY7: NF-kappaB p65 subunit

NF-kappaB p65 subunit dimerization domain homodimer N202R mutation. Determined by X-ray diffraction at 1.49 Å resolution. Released 4 Dec 2002.

Method: X-ray diffraction
Resolution: 1.49 Å
Organism: Mus musculus
Chains: 2
Atoms: 1,944
Mol. weight: 26.49 kDa
Released: 4 Dec 2002

Explore 1MY7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MY7 contains 7 α-helices and 22 β-strands across 2 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, 11 β-strands

Element	Residues	Length	Sheet
β-strand	196-199	4	1
β-strand	203-205	3	2
β-strand	211-216	6	1
β-strand	225-230	6	2
β-strand	233-236	4	2
β-strand	238	1	1
α-helix	241-243	3
β-strand	244	1	1
β-strand	249-253	5	1
α-helix	254-257	4
β-strand	266-274	9	2
β-strand	279-280	2	2
α-helix	281-283	3
β-strand	284-289	6	2

Chain B: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	196-199	4	3
β-strand	203-205	3	4
β-strand	211-216	6	3
β-strand	225-230	6	4
β-strand	233-236	4	4
α-helix	237	1
β-strand	238	1	3
α-helix	241-243	3
β-strand	244-245	2	3
β-strand	249-253	5	3
α-helix	254-257	4
β-strand	266-274	9	4
β-strand	279-280	2	4
α-helix	281-283	3
β-strand	284-289	6	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
NF-kappaB p65 (RelA) subunit	A, B	protein	114	Mus musculus	Q04207 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1MY7_1 NF-kappaB p65 (RelA) subunit (chains A, B)
TAELKICRVNRRSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAI
VFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKR

Primary citation

Solvent exposed non-contacting amino acids play a critical role in NF-kappaB/IkappaB alpha complex formation. Huxford, T., Mishler, D., Phelps, C.B. et al. J Mol Biol (2002) 324:587-597. DOI 10.1016/S0022-2836(02)01149-X · PubMed

Other PDB entries of the same protein (UniProt Q04207 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1MY5 1.8 Å, NF-kappaB p65 subunit dimerization domain homodimer
9BDW 1.87 Å, NF-kappaB RelA homo-dimer bound to GC-centric kappaB DNA
9BDV 1.9 Å, NF-kappaB RelA homo-dimer bound to TA-centric kappaB DNA
1BFT 2.0 Å, Structure of nf-kb P65 homodimer bound to a kb site
9BDU 2.03 Å, NF-kappaB RelA homo-dimer bound to AT-centric kappaB DNA
9E6W 2.04 Å, NF-kappaB RelA homo-dimer bound to a kappaB site of Cxcl2 gene
1OY3 2.05 Å, Crystal structure of an ikbbeta/nf-kb P65 homodimer complex
6GGR 2.1 Å, Crystal structure of Salmonella zinc metalloprotease effector GtgA in complex with p65
1IKN 2.3 Å, Ikappabalpha/nf-kappab complex
2RAM 2.4 Å, A novel DNA recognition mode by nf-kb P65 homodimer
1K3Z 2.5 Å, X-ray crystal structure of the IkBb/NF-kB p65 homodimer complex
5U01 2.5 Å, Cooperative DNA binding by two RelA dimers

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