2OSC: Angiopoietin-1 receptor

Synthesis, Structural Analysis, and SAR Studies of Triazine Derivatives as Potent, Selective Tie-2 Inhibitors. Determined by X-ray diffraction at 2.8 Å resolution. Released 20 Mar 2007.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,071
Mol. weight: 36.7 kDa
Ligands: MUH
Released: 20 Mar 2007

Explore 2OSC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OSC contains 18 α-helices and 12 β-strands across 1 chain. 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: 18 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	838-841	4	1
β-strand	852-855	4	1
α-helix	864-879	16
β-strand	885	1	2
β-strand	888-891	4	1
β-strand	900-903	4	1
β-strand	909	1	2
α-helix	910-916	7
α-helix	919-922	4
α-helix	924-930	7
β-strand	932	1	3
α-helix	938-956	19
α-helix	967-969	3
β-strand	970-973	4	2
α-helix	974-976	3
β-strand	977-980	4	2
α-helix	1002-1004	3
α-helix	1007-1012	6
α-helix	1017-1032	16
α-helix	1036-1037	2
α-helix	1044-1050	7
α-helix	1051-1053	3
β-strand	1063	1	4
α-helix	1065-1074	10
α-helix	1079-1081	3
α-helix	1083-1084	2
α-helix	1085-1097	13
β-strand	1103	1	4
β-strand	1106	1	3
α-helix	1113-1115	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiopoietin-1 receptor	A	protein	317	Homo sapiens	Q02763 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2OSC_1 Angiopoietin-1 receptor (chains A)
KNNPDPTIYPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHR
DFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFA
IANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR
GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAEL
YEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTL
YEKFTYAGIDCSAEEAA

Ligands and cofactors

ID	Name	Formula	Copies
MUH	N-{4-methyl-3-[(3-pyrimidin-4-ylpyridin-2-yl)amino]phenyl}-3-(trifluoromethyl)b…	C24 H18 F3 N5 O	1

Primary citation

Synthesis, structural analysis, and SAR studies of triazine derivatives as potent, selective Tie-2 inhibitors. Hodous, B.L., Geuns-Meyer, S.D., Hughes, P.E. et al. Bioorg Med Chem Lett (2007) 17:2886-2889. DOI 10.1016/j.bmcl.2007.02.067 · 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…
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
2GY5 2.9 Å, Tie2 Ligand-Binding Domain Crystal Structure

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