2GY5: Tie2 Ligand-Binding Domain Crystal Structure

Tie2 Ligand-Binding Domain Crystal Structure. Determined by X-ray diffraction at 2.9 Å resolution. Released 6 Jun 2006.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,383
Mol. weight: 48.68 kDa
Ligands: NAG, NDG
Released: 6 Jun 2006

Explore 2GY5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2GY5 contains 14 α-helices and 50 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: 14 helices, 50 β-strands

Element	Residues	Length	Sheet
β-strand	26-29	4	1
β-strand	34-35	2	2
β-strand	40-46	7	1
β-strand	56-59	4	3
α-helix	70-72	3
β-strand	74-76	3	1
β-strand	83-88	6	1
β-strand	98-106	9	3
β-strand	109-117	9	3
β-strand	118-119	2	2
β-strand	124-125	2	4
β-strand	130-133	4	5
β-strand	139-145	7	4
β-strand	153-157	5	5
β-strand	160-165	6	5
α-helix	167-169	3
β-strand	173-178	6	4
α-helix	183-185	3
β-strand	187-193	7	5
α-helix	198-200	3
β-strand	202-208	7	5
β-strand	215-216	2	6
β-strand	222-223	2	6
α-helix	224-225	2
β-strand	232-233	2	7
β-strand	240-241	2	7
α-helix	242-243	2
β-strand	246-247	2	8
β-strand	253-254	2	8
β-strand	259-260	2	9
β-strand	266-267	2	9
β-strand	279-281	3	1
β-strand	286-288	3	1
α-helix	289-290	2
β-strand	291	1	10
β-strand	294	1	11
α-helix	296-298	3
β-strand	300	1	11
α-helix	302-303	2
β-strand	306	1	12
β-strand	309	1	10
α-helix	313	1
β-strand	314	1	12
α-helix	315	1
β-strand	322-324	3	13
β-strand	328-330	3	13
β-strand	336	1	14
β-strand	342	1	14
α-helix	346-347	2
β-strand	351-352	2	15
β-strand	358	1	16
β-strand	361-362	2	17
β-strand	364-366	3	18
β-strand	369-373	5	15
α-helix	380-382	3
β-strand	383-386	4	16
β-strand	392-393	2	16
β-strand	397-400	4	15
β-strand	405-408	4	15
β-strand	411-414	4	18
α-helix	416-418	3
β-strand	420-428	9	16
β-strand	431-439	9	16
β-strand	441-442	2	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiopoietin-1 receptor	A	protein	423	Homo sapiens	Q02763 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2GY5_1 Angiopoietin-1 receptor (chains A)
AMDLILINSLPLVSDAETSLTCIASGWRPHEPITIGRDFEALMNQHQDPLEVTQDVTREW
AKKVVWKREKASKINGAYFCEGRVRGEAIRIRTMKMRQQASFLPATLTMTVDKGDNVNIS
FKKVLIKEEDAVIYKNGSFIHSVPRHEVPDILEVHLPHAQPQDAGVYSARYIGGNLFTSA
FTRLIVRRCEAQKWGPECNHLCTACMNNGVCHEDTGECICPPGFMGRTCEKACELHTFGR
TCKERCSGQEGCKSYVFCLPDPYGCSCATGWKGLQCNEACHPGFYGPDCKLRCSCNNGEM
CDRFQGCLCSPGWQGLQCEREGIPRMTPKIVDLPDHIEVNSGKFNPICKASGWPLPTNEE
MTLVKPDGTVLHPKDFNHTDHFSVAIFTIHRILPPDSGVWVCSVNTVAGMVEKPFNISVK
VLP

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
NDG	2-acetamido-2-deoxy-alpha-D-glucopyranose	C8 H15 N O6	4

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

Primary citation

Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex. Barton, W.A., Tzvetkova-Robev, D., Miranda, E.P. et al. Nat Struct Mol Biol (2006) 13:524-532. DOI 10.1038/nsmb1101 · 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
2OSC 2.8 Å, Synthesis, Structural Analysis, and SAR Studies of Triazine Derivatives as Potent,…

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