1FVR: TIE2 kinase domain

TIE2 kinase domain. Determined by X-ray diffraction at 2.2 Å resolution. Released 20 Sept 2001.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,201
Mol. weight: 75.06 kDa
Released: 20 Sept 2001

Explore 1FVR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FVR contains 44 α-helices and 40 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: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	818	1	1
α-helix	819-820	2
α-helix	821-823	3
β-strand	825-831	7	1
β-strand	832	1	2
β-strand	834	1	2
β-strand	837-845	9	1
β-strand	848-858	11	1
α-helix	868-876	9
β-strand	885	1	3
α-helix	886-887	2
β-strand	888-894	7	1
β-strand	897-902	6	1
β-strand	909	1	3
α-helix	910-915	6
α-helix	919-922	4
α-helix	924-929	6
β-strand	932	1	4
α-helix	938-957	20
β-strand	960-961	2	5
α-helix	967-969	3
β-strand	970-972	3	3
α-helix	974-976	3
β-strand	978-980	3	3
β-strand	986-987	2	5
β-strand	991-992	2	6
α-helix	1007-1012	6
β-strand	1014-1015	2	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	7
α-helix	1065-1074	10
α-helix	1079-1081	3
α-helix	1083-1084	2
α-helix	1085-1097	13
β-strand	1103	1	7
β-strand	1106	1	4
α-helix	1113-1115	3
α-helix	1118-1120	3

Chain B: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	818	1	1
α-helix	819-820	2
α-helix	821-823	3
β-strand	825-831	7	1
β-strand	832	1	8
β-strand	834	1	8
β-strand	837-845	9	1
β-strand	848-858	11	1
α-helix	868-877	10
β-strand	885	1	9
α-helix	886-887	2
β-strand	888-894	7	1
β-strand	897-902	6	1
β-strand	909	1	9
α-helix	910-916	7
α-helix	919-922	4
α-helix	924-929	6
β-strand	932	1	10
α-helix	938-956	19
β-strand	960-961	2	11
α-helix	967-969	3
β-strand	970-972	3	9
α-helix	974-976	3
β-strand	978-980	3	9
β-strand	986-987	2	11
β-strand	991-992	2	12
α-helix	1002-1004	3
α-helix	1007-1012	6
β-strand	1014-1015	2	12
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	13
α-helix	1065-1074	10
α-helix	1079-1081	3
α-helix	1083-1084	2
α-helix	1085-1097	13
β-strand	1103	1	13
β-strand	1106	1	10
α-helix	1113-1115	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine-protein kinase tie-2	A, B	protein	327	Homo sapiens	Q02763 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1FVR_1 TYROSINE-PROTEIN KINASE TIE-2 (chains A, B)
MKKHHHHHHGKNNPDPTIYPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRM
KEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKS
RVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV
AKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGT
PYCGMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE
ERKTYVNTTLYEKFTYAGIDCSAEEAA

Primary citation

Structure of the Tie2 RTK domain: self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail. Shewchuk, L.M., Hassell, A.M., Ellis, B. et al. Structure (2000) 8:1105-1113. DOI 10.1016/S0969-2126(00)00516-5 · 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
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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