6MWE: TIE2

Crystal structure of TIE2 in complex with decipera compound DP1919. Determined by X-ray diffraction at 2.05 Å resolution. Released 21 Nov 2018.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,773
Mol. weight: 74 kDa
Ligands: 919
Released: 21 Nov 2018

Explore 6MWE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6MWE contains 46 α-helices and 28 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: 23 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	818	1	1
α-helix	821-823	3
β-strand	824-833	10	1
β-strand	836-845	10	1
β-strand	848-856	9	1
α-helix	872-879	8
β-strand	885	1	2
α-helix	886-887	2
β-strand	888-894	7	1
β-strand	897-903	7	1
β-strand	909	1	2
α-helix	910-916	7
α-helix	919-922	4
α-helix	924-929	6
β-strand	932	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	985-987	3
α-helix	1000-1004	5
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	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
α-helix	1118-1120	3

Chain B: 23 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	818	1	5
α-helix	821-823	3
β-strand	824-833	10	5
β-strand	836-845	10	5
β-strand	848-855	8	5
α-helix	872-879	8
β-strand	885	1	6
α-helix	886-887	2
β-strand	888-893	6	5
β-strand	898-903	6	5
β-strand	909	1	6
α-helix	910-916	7
α-helix	919-922	4
α-helix	924-929	6
β-strand	932	1	7
α-helix	938-957	20
α-helix	967-969	3
β-strand	970-972	3	6
α-helix	974-976	3
β-strand	978-980	3	6
α-helix	985-987	3
α-helix	1000-1004	5
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	8
α-helix	1065-1074	10
α-helix	1079-1081	3
α-helix	1083-1084	2
α-helix	1085-1097	13
β-strand	1103	1	8
β-strand	1106	1	7
α-helix	1113-1115	3
α-helix	1118-1120	3

Molecules and chains

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

Sequence of entity 1 (A, B), FASTA

>6MWE_1 Angiopoietin-1 receptor (chains A, B)
KNNPDPTIYPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHR
DFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFA
IANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR
GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAEL
YEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTL
YEKFTYAGIDCSAEEAA

Ligands and cofactors

ID	Name	Formula	Copies
919	4-[4-({[3-tert-butyl-1-(quinolin-6-yl)-1H-pyrazol-5-yl]carbamoyl}amino)-3-fluor…	C30 H28 F N7 O3	2

Water and common crystallization additives (SO4) are not listed.

Primary citation

The Selective Tie2 Inhibitor Rebastinib Blocks Recruitment and Function of Tie2. Harney, A.S., Karagiannis, G.S., Pignatelli, J. et al. Mol Cancer Ther (2017) 16:2486-2501. DOI 10.1158/1535-7163.MCT-17-0241 · 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
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
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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