1F3V: PDB entry 1F3V

Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 Sept 2000.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,749
Mol. weight: 39.13 kDa
Released: 6 Sept 2000

Explore 1F3V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F3V contains 16 α-helices and 18 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: 8 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	12-21	10	1
α-helix	28-33	6
α-helix	38-48	11
α-helix	49-53	5
β-strand	59-66	8	1
β-strand	71-78	8	1
α-helix	80-91	12
α-helix	94-106	13
β-strand	114-120	7	1
β-strand	123-124	2	1
α-helix	125-128	4
α-helix	132-141	10
β-strand	146	1	2
α-helix	150-162	13

Chain B: 8 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	332-347	16
β-strand	353-359	7	3
α-helix	361-369	9
β-strand	376-377	2	4
α-helix	378-380	3
β-strand	381-382	2	4
β-strand	389-395	7	4
α-helix	400-402	3
β-strand	406-414	9	4
α-helix	419-421	3
β-strand	430-434	5	3
β-strand	443-447	5	3
β-strand	449	1	2
α-helix	454-456	3
α-helix	458-459	2
β-strand	463	1	4
β-strand	467-474	8	4
α-helix	475-478	4
β-strand	486	1	3
β-strand	489-496	8	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor necrosis factor receptor type 1 associated death domain protein	A	protein	179	Homo sapiens	Q15628 (AlphaFold model)
Tumor necrosis factor receptor-associated protein	B	protein	171	Homo sapiens	Q12933 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1F3V_1 TUMOR NECROSIS FACTOR RECEPTOR TYPE 1 ASSOCIATED DEATH DOMAIN PROTEIN (chains A)
MAAGQNGHEEWVGSAYLFVESSLDKVVLSDAYAHPQQKVAVYRALQAALAESGGSPDVLQ
MLKIHRSDPQLIVQLRFCGRQPCGRFLRAYREGALRAALQRSLAAALAQHSVPLQLELRA
GAERLDALLADEERCLSCILAQQPDRLRDEELAELEDALRNLKCGSGARGGDGEVASAP

Sequence of entity 2 (B), FASTA

>1F3V_2 TUMOR NECROSIS FACTOR RECEPTOR-ASSOCIATED PROTEIN (chains B)
KDLAMADLEQKVLEMEASTYDGVFIWKISDFPRKRQEAVAGRIPAIFSPAFYTSRYGYKM
CLRIYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPD
VTSSSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL

Primary citation

A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction. Park, Y.C., Ye, H., Hsia, C. et al. Cell (2000) 101:777-787. DOI 10.1016/S0092-8674(00)80889-2 · PubMed

Other PDB entries of the same protein (UniProt Q15628 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6AC0 1.45 Å, Crystal structure of TRADD death domain GlcNAcylated by EPEC effector NleB
9VGD 3.3 Å, Helical assembly of TRADD death domain
9VIN 3.41 Å, Ternary complex of TNFR1-DD, TRADD-DD and RIPK1-DD
1F2H Solution structure of the N-terminal domain of the TNFR1 associated protein, tradd.
5XME Solution structure of C-terminal domain of TRADD
7CSQ Solution structure of the complex between p75NTR-DD and TRADD-DD

Browse structure collections

About this viewer

MolViewer shows 1F3V directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.