Research workbench

Structure of the DNA binding domains of nfat, fos and jun bound to DNA

Analyse Structure of the DNA binding domains of nfat, fos and jun bound to DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1A02
Type: protein + DNA
Length: 425 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q13469, P01100, P05412

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	dna	20	—	—
B	—	dna	20	—	—
N	—	protein	280	—	Q13469
F	—	protein	53	—	P01100
J	—	protein	52	—	P05412

Compared structures

1A02 · Structure of the DNA binding domains of nfat, fos and jun bound to DNA · the same entry in another collection · chain J against J, TM-score 1.00
P01100 · AlphaFold monomer V2.0 prediction for proto-oncogene C-fos (P01100) · a predicted model of the same protein · chain F against A, TM-score 0.91
P05412 · AlphaFold monomer V2.0 prediction for transcription factor ap-1 (P05412) · a predicted model of the same protein · chain J against A, TM-score 0.69
Q13469 · AlphaFold monomer V2.0 prediction for nuclear factor of activated T-cells, cytoplasmic 2… · a predicted model of the same protein · chain N against A, TM-score 0.64

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 Q13469
Every structure of UniProt P01100
Every structure of UniProt P05412
Elsewhere: RCSB PDB 1A02 · PDBe 1A02 · UniProt Q13469 · UniProt P01100 · UniProt P05412

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