9LV4: Human Tie2/minibinder tw1102_4 helices Complex

Cryo-EM Structure of Human Tie2/minibinder tw1102_4 helices Complex. Determined by electron microscopy at 2.67 Å resolution. Released 18 Feb 2026.

Method: Electron microscopy
Resolution: 2.67 Å
Organisms: Homo sapiens, synthetic construct
Chains: 2
Atoms: 3,549
Mol. weight: 61.9 kDa
Released: 18 Feb 2026

Explore 9LV4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9LV4 contains 12 α-helices and 33 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: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	10-26	17
α-helix	35-48	14
α-helix	53-66	14
α-helix	75-89	15

Chain B: 8 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	26-30	5	1
β-strand	40-46	7	1
α-helix	54-55	2
β-strand	56-59	4	2
α-helix	70-72	3
β-strand	74	1	1
β-strand	83-88	6	1
β-strand	98-104	7	2
β-strand	111-117	7	2
β-strand	132-133	2	3
β-strand	139-144	6	4
β-strand	153-157	5	5
β-strand	160-165	6	5
β-strand	173-178	6	4
α-helix	183-185	3
β-strand	188-193	6	5
β-strand	204-205	2	5
β-strand	207-208	2	3
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
β-strand	246-247	2	8
β-strand	253-254	2	8
β-strand	260	1	9
β-strand	266	1	9
β-strand	278-280	3	1
β-strand	287-289	3	1
α-helix	296-298	3
α-helix	309-311	3
α-helix	346-347	2
β-strand	352	1	10
β-strand	358	1	11
β-strand	369-372	4	10
α-helix	380-382	3
β-strand	383-384	2	11
β-strand	398-399	2	10
β-strand	405-408	4	10
β-strand	420-428	9	11
β-strand	431-439	9	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiopoietin-1 receptor	B	protein	430	Homo sapiens	Q02763 (AlphaFold model)
Minibinder tw1102	A	protein	125	synthetic construct

Sequence of entity 1 (B), FASTA

>9LV4_1 Angiopoietin-1 receptor (chains B)
AMDLILINSLPLVSDAETSLTCIASGWRPHEPITIGRDFEALMNQHQDPLEVTQDVTREW
AKKVVWKREKASKINGAYFCEGRVRGEAIRIRTMKMRQQASFLPATLTMTVDKGDNVNIS
FKKVLIKEEDAVIYKNGSFIHSVPRHEVPDILEVHLPHAQPQDAGVYSARYIGGNLFTSA
FTRLIVRRCEAQKWGPECNHLCTACMNNGVCHEDTGECICPPGFMGRTCEKACELHTFGR
TCKERCSGQEGCKSYVFCLPDPYGCSCATGWKGLQCNEACHPGFYGPDCKLRCSCNNGEM
CDRFQGCLCSPGWQGLQCEREGIPRMTPKIVDLPDHIEVNSGKFNPICKASGWPLPTNEE
MTLVKPDGTVLHPKDFNHTDHFSVAIFTIHRILPPDSGVWVCSVNTVAGMVEKPFNISVK
VLPKPLNAPN

Sequence of entity 2 (A), FASTA

>9LV4_2 Minibinder tw1102 (chains A)
MSGSEEEQKLVEEAIEKLTKILEELAKKYGEKMKEPKEYYLRMSEKIKKNEQPEQDMAIL
IHNAGKEVLKLTGDEEAALELAKLSAKLFQYAGDTDGAVRALKQSGIGEEAEKIAEEIRK
KAAGS

Primary citation

Designed Tie2-specific minibinder with therapeutic potential. Fu, Y., Kim, H.M. To be published.

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
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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