1EXT: Tumor necrosis factor receptor

Extracellular domain of the 55KDA tumor necrosis factor receptor. Crystallized at PH3.7 in P 21 21 21. Determined by X-ray diffraction at 1.85 Å resolution. Released 11 Jan 1997.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,887
Mol. weight: 36.98 kDa
Ligands: MG
Released: 11 Jan 1997

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

Secondary structure: helices and β-sheets

1EXT contains 22 α-helices and 40 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: 12 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	19-21	3	1
β-strand	29-31	3	1
α-helix	32	1
β-strand	33	1	2
α-helix	34	1
β-strand	37-41	5	3
α-helix	49-50	2
β-strand	51-54	4	3
α-helix	55-56	2
β-strand	59-60	2	4
β-strand	65	1	2
α-helix	70	1
β-strand	71-72	2	4
α-helix	73-74	2
α-helix	78-80	3
β-strand	83-86	4	5
β-strand	89	1	6
β-strand	92	1	6
β-strand	95-97	3	5
β-strand	102-108	7	7
β-strand	111-116	6	7
α-helix	117-118	2
β-strand	123-127	5	8
β-strand	130	1	9
β-strand	133	1	9
β-strand	136-139	4	8
α-helix	140	1
β-strand	143-146	4	10
β-strand	149-152	4	10
α-helix	153-155	3
α-helix	163-166	4
α-helix	168-169	2

Chain B: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	19-21	3	11
β-strand	29-31	3	11
α-helix	32	1
β-strand	33	1	12
α-helix	34	1
β-strand	37-41	5	13
β-strand	51-54	4	13
α-helix	55-56	2
β-strand	59-60	2	14
β-strand	65	1	12
α-helix	70	1
β-strand	71-72	2	14
α-helix	73-74	2
α-helix	78-80	3
β-strand	83-86	4	15
β-strand	89	1	16
β-strand	92	1	16
β-strand	95-97	3	15
β-strand	102-108	7	17
β-strand	111-116	6	17
α-helix	117-118	2
β-strand	123-127	5	18
β-strand	130	1	19
β-strand	133	1	19
β-strand	136-139	4	18
α-helix	140	1
β-strand	143-146	4	20
β-strand	149-152	4	20
α-helix	153-155	3
α-helix	164-166	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor necrosis factor receptor	A, B	protein	162	Homo sapiens	P19438 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1EXT_1 TUMOR NECROSIS FACTOR RECEPTOR (chains A, B)
MDSVCPQGKYIHPQNNSICCTKCHKGTYLYNDCPGPGQDTDCRECESGSFTASENHLRHC
LSCSKCRKEMGQVEISSCTVDRDTVCGCRKNQYRHYWSENLFQCFNCSLCLNGTVHLSCQ
EKQNTVCTCHAGFFLRENECVSCSNCKKSLECTKLCLPQIEN

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structures of the extracellular domain of the type I tumor necrosis factor receptor. Naismith, J.H., Devine, T.Q., Kohno, T. et al. Structure (1996) 4:1251-1262. DOI 10.1016/S0969-2126(96)00134-7 · PubMed

Other PDB entries of the same protein (UniProt P19438 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8P6Q 1.4 Å, Racemic structure of TNFR1 cysteine-rich domain
9S3I 1.64 Å, Crystal structure of the human tumor necrosis factor receptor 1 extracellular domain at…
9S3J 1.77 Å, Crystal structure of the human tumor necrosis factor receptor 1 extracellular domain in…
1NCF 2.25 Å, A new paradigm for tumor necrosis factor signalling
8ZUI 2.56 Å, Binary cluster of TNF-TNFR1 ectodomain complex
9V9C 2.62 Å, Cryo-EM structure of human TNFR1 DD filament
7KP7 2.65 Å, asymmetric mTNF-alpha hTNFR1 complex
1TNR 2.85 Å, Crystal structure of the soluble human 55 kd tnf receptor-human tnf-beta complex:…
1FT4 2.9 Å, Photochemically-enhanced binding of small molecules to the tumor necrosis factor…
7KPB 3.0 Å, Human TNF-alpha TNFR1 complex bound to conformationally selective antibody
7KP8 3.15 Å, asymmetric mTNF-alpha hTNFR1 complex
9VIN 3.41 Å, Ternary complex of TNFR1-DD, TRADD-DD and RIPK1-DD

Browse structure collections

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