2OO8: Angiopoietin-1 receptor

Synthesis, Structural Analysis, and SAR Studies of Triazine Derivatives as Potent, Selective Tie-2 Inhibitors. Determined by X-ray diffraction at 2.2 Å resolution. Released 20 Mar 2007.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,160
Mol. weight: 36.79 kDa
Ligands: RAJ
Released: 20 Mar 2007

Explore 2OO8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OO8 contains 19 α-helices and 14 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 X: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	837-842	6	1
β-strand	851-856	6	1
α-helix	864-877	14
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
β-strand	918	1	3
α-helix	919-922	4
α-helix	924-929	6
β-strand	932	1	4
β-strand	934	1	3
α-helix	938-956	19
α-helix	967-969	3
β-strand	970-972	3	2
α-helix	974-976	3
β-strand	978-980	3	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
α-helix	1057-1060	4
β-strand	1063	1	5
α-helix	1065-1074	10
α-helix	1079-1081	3
α-helix	1083-1084	2
α-helix	1085-1097	13
β-strand	1103	1	5
β-strand	1106	1	4
α-helix	1113-1115	3

Molecules and chains

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

Sequence of entity 1 (X), FASTA

>2OO8_1 Angiopoietin-1 receptor (chains X)
KNNPDPTIYPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHR
DFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFA
IANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR
GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAEL
YEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTL
YEKFTYAGIDCSAEEAA

Ligands and cofactors

ID	Name	Formula	Copies
RAJ	N-{3-[3-(dimethylamino)propyl]-5-(trifluoromethyl)phenyl}-4-methyl-3-[(3-pyrimi…	C29 H29 F3 N6 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
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
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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