1RF3: TNF receptor associated factor 3

Structurally Distinct Recognition Motifs in Lymphotoxin-B Receptor and CD40 for TRAF-mediated Signaling. Determined by X-ray diffraction at 3.5 Å resolution. Released 6 Jul 2004.

Method
X-ray diffraction
Resolution
3.5 Å
Organism
Homo sapiens
Chains
2
Atoms
1,709
Mol. weight
25.42 kDa
Released
6 Jul 2004

Explore 1RF3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1RF3 contains 4 α-helices and 15 β-strands across 1 chain. 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: 4 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix316-34025
α-helix344-3474
β-strand355-35951
α-helix361-37010
β-strand37612
β-strand381-38223
β-strand389-39023
β-strand393-39532
β-strand408-41032
β-strand41313
β-strand41414
β-strand43015
β-strand432-43431
β-strand445-44621
β-strand46414
β-strand47212
α-helix476-4805
β-strand489-49351
β-strand49615

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
TNF receptor associated factor 3Aprotein200Homo sapiensQ13114 (AlphaFold model)
24-residue peptide from Lymphotoxin-B ReceptorBprotein24P36941 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1RF3_1 TNF receptor associated factor 3 (chains A)
NTGLLESQLSRHDQMLSVHDIRLADMDLRFQVLETASYNGVLIWKIRDYKRRKQEAVMGK
TLSLYSQPFYTGYFGYKMCARVYLNGDGMGKGTHLSLFFVIMRGEYDALLPWPFKQKVTL
MLMDQGSSRRHLGDAFKPDPNSSSFKKPTGEMNIASGCPVFVAQTVLENGTYIKDDTIFI
KVIVDTSDLPDPLEHHHHHH
Sequence of entity 2 (B), FASTA
>1RF3_2 24-residue peptide from Lymphotoxin-B Receptor (chains B)
PYPIPEEGDPGPPGLSTPHQEDGK

Primary citation

Structurally distinct recognition motifs in lymphotoxin-beta receptor and CD40 for tumor necrosis factor receptor-associated factor (TRAF)-mediated signaling. Li, C., Norris, P.S., Ni, C.Z. et al. J Biol Chem (2003) 278:50523-50529. DOI 10.1074/jbc.M309381200 · PubMed

Other PDB entries of the same protein (UniProt Q13114 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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