4X3J: Angiopoietin-1 receptor

Selection of fragments for kinase inhibitor design: decoration is key. Determined by X-ray diffraction at 2.5 Å resolution. Released 24 Dec 2014.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,936
Mol. weight: 37.25 kDa
Ligands: 3WR
Released: 24 Dec 2014

Explore 4X3J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4X3J 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	839-841	3	1
β-strand	852-854	3	1
α-helix	873-878	6
β-strand	885	1	2
α-helix	886-887	2
β-strand	888	1	1
β-strand	901-903	3	1
β-strand	909	1	2
α-helix	910-916	7
β-strand	918	1	3
α-helix	919-922	4
α-helix	924-930	7
β-strand	934	1	3
α-helix	938-957	20
α-helix	967-969	3
β-strand	970-972	3	2
α-helix	974-976	3
β-strand	978-980	3	2
α-helix	1007-1012	6
α-helix	1017-1032	16
α-helix	1036-1037	2
α-helix	1044-1050	7
α-helix	1057-1060	4
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
α-helix	1113-1115	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiopoietin-1 receptor	A	protein	321	Homo sapiens	Q02763 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4X3J_1 Angiopoietin-1 receptor (chains A)
ALNRKVKNNPDPTIYPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYA
SKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLE
TDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRNLAARNILVGENYVAKIA
DFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCG
MTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKT
YVNTTLYEKFTYAGIDCSAEE

Ligands and cofactors

ID	Name	Formula	Copies
3WR	1-[4-(4-amino-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl)phenyl]-3-[2-fluoro-5-(trifl…	C21 H14 F4 N6 O2	1

Primary citation

Selection of fragments for kinase inhibitor design: decoration is key. Czodrowski, P., Holzemann, G., Barnickel, G. et al. J Med Chem (2015) 58:457-465. DOI 10.1021/jm501597j · 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…
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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