5UTK: Angiopoietin-1 receptor

Crystal structure of the membrane proximal three fibronectin type III (FNIII) domains of Tie2 (Tie2[FNIIIa-c]). Determined by X-ray diffraction at 2.5 Å resolution. Released 12 Apr 2017.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,492
Mol. weight: 68.27 kDa
Released: 12 Apr 2017

Explore 5UTK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5UTK contains 17 α-helices and 51 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: 9 helices, 25 β-strands

Element	Residues	Length	Sheet
α-helix	443-445	3
β-strand	446-447	2	1
β-strand	452-456	5	2
β-strand	461-464	4	2
β-strand	470-471	2	1
β-strand	476-485	10	3
α-helix	491-492	2
β-strand	493-497	5	3
β-strand	501-504	4	2
β-strand	512-521	10	3
β-strand	527	1	3
β-strand	534-537	4	3
α-helix	539-546	8
β-strand	550-553	4	4
β-strand	559-562	4	4
α-helix	564-566	3
β-strand	575-581	7	5
β-strand	589-594	6	5
β-strand	599-602	4	4
β-strand	610-618	9	5
α-helix	622-628	7
β-strand	629-632	4	5
α-helix	633-635	3
α-helix	638-642	5
β-strand	643-648	6	6
β-strand	655-660	6	6
β-strand	669-676	8	7
β-strand	685-689	5	7
β-strand	696-699	4	6
β-strand	707-715	9	7
β-strand	720	1	7
α-helix	721-723	3
β-strand	724-730	7	7
α-helix	731-733	3

Chain B: 8 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	443-445	3
β-strand	446-447	2	8
β-strand	452-456	5	9
β-strand	461-464	4	9
β-strand	470-471	2	8
β-strand	478-485	8	10
α-helix	491-492	2
β-strand	493-496	4	10
β-strand	501-504	4	9
β-strand	512-520	9	10
β-strand	527	1	10
β-strand	534-537	4	10
α-helix	539-546	8
β-strand	550-553	4	11
β-strand	559-562	4	11
β-strand	575-580	6	12
β-strand	591-594	4	12
β-strand	599-602	4	11
β-strand	610-618	9	12
α-helix	622-628	7
β-strand	629-632	4	12
α-helix	633-635	3
α-helix	638-642	5
β-strand	643-648	6	13
β-strand	655-660	6	13
β-strand	669-676	8	14
β-strand	685-689	5	14
β-strand	696-699	4	13
α-helix	702-703	2
β-strand	707-715	9	14
β-strand	720	1	14
β-strand	724-725	2	14
β-strand	729-730	2	14
α-helix	731-733	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiopoietin-1 receptor	A, B	protein	304	Homo sapiens	Q02763 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5UTK_1 Angiopoietin-1 receptor (chains A, B)
GSGSKVLPKPLNAPNVIDTGHNFAVINISSEPYFGDGPIKSKKLLYKPVNHYEAWQHIQV
TNEIVTLNYLEPRTEYELCVQLVRRGEGGEGHPGPVRRFTTASIGLPPPRGLNLLPKSQT
TLNLTWQPIFPSSEDDFYVEVERRSVQKSDQQNIKVPGNLTSVLLNNLHPREQYMVRARV
NTKAQGEWSEDLTAWTLSDILPPQPENIKISNITHSSAMISWTILDGYSISSITIRYKVQ
GKNEDQHVDVKIKNATITQYQLKGLEPETAYQVDIFAENNIGSSNPAFSHELVTLPESQA
PADL

Primary citation

Dimerization of Tie2 mediated by its membrane-proximal FNIII domains. Moore, J.O., Lemmon, M.A., Ferguson, K.M. Proc Natl Acad Sci U S A (2017) 114:4382-4387. DOI 10.1073/pnas.1617800114 · PubMed

Other PDB entries of the same protein (UniProt Q02763 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3BEA 2.02 Å, cFMS tyrosine kinase (tie2 KID) in complex with a pyrimidinopyridone inhibitor
6MWE 2.05 Å, Crystal structure of TIE2 in complex with decipera compound DP1919
7E72 2.09 Å, Crystal structure of Tie2-agonistic antibody in complex with human Tie2 Fn2-3
1FVR 2.2 Å, TIE2 kinase domain
2OO8 2.2 Å, Synthesis, Structural Analysis, and SAR Studies of Triazine Derivatives as Potent,…
3L8P 2.4 Å, Crystal structure of cytoplasmic kinase domain of Tie2 complexed with inhibitor CEP11207
2P4I 2.5 Å, Evolution of a highly Selective and Potent 2-(Pyridin-2-yl)-1,3,5-triazine Tie-2 Kinase…
4X3J 2.5 Å, Selection of fragments for kinase inhibitor design: decoration is key
5MYB 2.6 Å, Homodimerization of Tie2 Fibronectin-like domains 2 and 3 in space group P21
9LV4 2.67 Å, Cryo-EM Structure of Human Tie2/minibinder tw1102_4 helices Complex
2OSC 2.8 Å, Synthesis, Structural Analysis, and SAR Studies of Triazine Derivatives as Potent,…
2GY5 2.9 Å, Tie2 Ligand-Binding Domain Crystal Structure

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