5MYB: Angiopoietin-1 receptor

Homodimerization of Tie2 Fibronectin-like domains 2 and 3 in space group P21. Determined by X-ray diffraction at 2.6 Å resolution. Released 26 Apr 2017.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,123
Mol. weight: 77.06 kDa
Ligands: NAG
Released: 26 Apr 2017

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

Secondary structure: helices and β-sheets

5MYB contains 13 α-helices and 30 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: 6 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	544-546	3
β-strand	550-553	4	1
β-strand	559-562	4	1
β-strand	575-582	8	2
β-strand	588-594	7	2
β-strand	599-602	4	1
β-strand	610-618	9	2
β-strand	622	1	2
α-helix	623-625	3
α-helix	627-628	2
β-strand	629-632	4	2
α-helix	633-635	3
α-helix	638-642	5
β-strand	643-648	6	3
β-strand	654-660	7	3
β-strand	669-676	8	4
β-strand	683-689	7	4
β-strand	696-700	5	3
α-helix	702-703	2
β-strand	707-715	9	4
β-strand	720	1	4
β-strand	727-730	4	4

Chain B: 7 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	543-546	4
β-strand	550-553	4	5
β-strand	559-562	4	5
α-helix	571	1
α-helix	573	1
β-strand	575-582	8	6
β-strand	588-594	7	6
β-strand	599-602	4	5
β-strand	610-618	9	6
α-helix	624-628	5
β-strand	629-632	4	6
α-helix	633-635	3
α-helix	638-642	5
β-strand	643-648	6	7
β-strand	654-660	7	7
β-strand	667-676	10	4
β-strand	683-689	7	4
β-strand	696-700	5	7
α-helix	702-703	2
β-strand	708-716	9	4
β-strand	727-729	3	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiopoietin-1 receptor	A, B	protein	333	Homo sapiens	Q02763 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5MYB_1 Angiopoietin-1 receptor (chains A, B)
MKFLVNVALVFMVVYISYIYADPVLPKPLNAPNVIDTGHNFAVINISSEPYFGDGPIKSK
KLLYKPVNHYEAWQHIQVTNEIVTLNYLEPRTEYELCVQLVRRGEGGEGHPGPVRRFTTA
SIGLPPPRGLNLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQKSDQQNIKVPGNLTS
VLLNNLHPREQYVVRARVNTKAQGEWSEDLTAWTLSDILPPQPENIKISNITHSSAVISW
TILDGYSISSITIRYKVQGKNEDQHVDVKIKNATITQYQLKGLEPETAYQVDIFAENNIG
SSNPAFSHELVTLPESQAPADLGIEGRHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	4

Primary citation

Structural basis of Tie2 activation and Tie2/Tie1 heterodimerization. Leppanen, V.M., Saharinen, P., Alitalo, K. Proc Natl Acad Sci U S A (2017) 114:4376-4381. DOI 10.1073/pnas.1616166114 · 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
5UTK 2.5 Å, Crystal structure of the membrane proximal three fibronectin type III (FNIII) domains of…
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

Browse structure collections

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