1FLK: Tnf receptor associated factor 3

Molecular basis for CD40 signaling mediated by TRAF3. Determined by X-ray diffraction at 2.8 Å resolution. Released 18 Oct 2000.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,252
Mol. weight: 51.77 kDa
Released: 18 Oct 2000

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

Secondary structure: helices and β-sheets

1FLK contains 13 α-helices and 26 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: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	310-346	37
β-strand	353-359	7	1
α-helix	361-369	9
β-strand	376-377	2	2
α-helix	378-380	3
β-strand	381-382	2	3
β-strand	389-390	2	3
β-strand	392-395	4	2
α-helix	400-402	3
β-strand	406-411	6	2
β-strand	414	1	4
β-strand	430-434	5	1
β-strand	444-448	5	1
β-strand	464	1	4
β-strand	470-475	6	2
α-helix	476-479	4
β-strand	489-495	7	1

Chain B: 8 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	301-303	3
α-helix	304-307	4
α-helix	310-346	37
β-strand	353	1	5
β-strand	356-359	4	6
α-helix	361-369	9
β-strand	376-377	2	7
α-helix	378-380	3
β-strand	381-382	2	7
β-strand	389-395	7	7
β-strand	406-414	9	7
α-helix	428-429	2
β-strand	430-435	6	6
α-helix	442-443	2
β-strand	444-448	5	6
β-strand	464	1	7
β-strand	468-475	8	7
α-helix	476-480	5
β-strand	486	1	6
β-strand	489-493	5	6
β-strand	495	1	5
β-strand	496	1	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tnf receptor associated factor 3	A, B	protein	228	Homo sapiens	Q13114 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1FLK_1 TNF RECEPTOR ASSOCIATED FACTOR 3 (chains A, B)
RQNWEEADSMKSSVESLQNRVTELESVDKSAGQVARNTGLLESQLSRHDQMLSVHDIRLA
DMDLRFQVLETASYNGVLIWKIRDYKRRKQEAVMGKTLSLYSQPFYTGYFGYKMCARVYL
NGDGMGKGTHLSLFFVIMRGEYDALLPWPFKQKVTLMLMDQGSSRRHLGDAFKPDPNSSS
FKKPTGEMNIASGCPVFVAQTVLENGTYIKDDTIFIKVIVDTSDLPDP

Primary citation

Molecular basis for CD40 signaling mediated by TRAF3. Ni, C.Z., Welsh, K., Leo, E. et al. Proc Natl Acad Sci U S A (2000) 97:10395-10399. DOI 10.1073/pnas.97.19.10395 · PubMed

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

8T5P 2.5 Å, SARS-CoV-2 ORF3a peptide in complex with TRAF3 TRAF domain
2GKW 2.7 Å, Key contacts promote recongnito of BAFF-R by TRAF3
1ZMS 2.8 Å, LMP1 Protein binds to TRAF3 as a structural CD40
8ZUK 2.83 Å, Cluster structure of the BAFF-BAFFR-TRAF3 complex
1L0A 2.9 Å, Downstream regulator tank binds to the CD40 recognition site on TRAF3
1FLL 3.5 Å, Molecular basis for CD40 signaling mediated by TRAF3
1KZZ 3.5 Å, Downstream regulator tank binds to the CD40 recognition site on TRAF3
1RF3 3.5 Å, Structurally Distinct Recognition Motifs in Lymphotoxin-B Receptor and CD40 for…
2ECY Solution structure of the Zinc finger, C3HC4 type (RING finger)" domain of TNF…

Browse structure collections

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