7E72: Tie2-agonistic antibody
Crystal structure of Tie2-agonistic antibody in complex with human Tie2 Fn2-3. Determined by X-ray diffraction at 2.09 Å resolution. Released 10 Nov 2021.
- Method
- X-ray diffraction
- Resolution
- 2.09 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 10,494
- Mol. weight
- 142.43 kDa
- Released
- 10 Nov 2021
Explore 7E72 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7E72 contains 57 α-helices and 118 β-strands across 6 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: 12 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-5 | 3 | 1 |
| β-strand | 9-12 | 4 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 58-60 | 3 | 2 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 1 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 2 |
| β-strand | 104-105 | 2 | 2 |
| β-strand | 109-113 | 5 | 2 |
| α-helix | 116-118 | 3 | |
| β-strand | 119 | 1 | 3 |
| α-helix | 120-121 | 2 | |
| β-strand | 122-126 | 5 | 4 |
| α-helix | 127-129 | 3 | |
| β-strand | 137-147 | 11 | 4 |
| β-strand | 148 | 1 | 3 |
| β-strand | 153-156 | 4 | 5 |
| α-helix | 157-159 | 3 | |
| β-strand | 161 | 1 | 5 |
| β-strand | 165-167 | 3 | 4 |
| α-helix | 168-170 | 3 | |
| β-strand | 171-172 | 2 | 4 |
| β-strand | 178-187 | 10 | 4 |
| α-helix | 188-190 | 3 | |
| β-strand | 197-202 | 6 | 5 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-212 | 6 | 5 |
| α-helix | 215-217 | 3 | |
Chain B: 9 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-13 | 4 | 7 |
| β-strand | 19-25 | 7 | 6 |
| β-strand | 33-38 | 6 | 7 |
| β-strand | 44-49 | 6 | 7 |
| β-strand | 53-54 | 2 | 7 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 6 |
| β-strand | 70-75 | 6 | 6 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 7 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 7 |
| β-strand | 102-106 | 5 | 7 |
| β-strand | 111 | 1 | 8 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 9 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 9 |
| β-strand | 140 | 1 | 8 |
| β-strand | 145-150 | 6 | 10 |
| β-strand | 153-154 | 2 | 10 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 9 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 9 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 10 |
| β-strand | 205-210 | 6 | 10 |
Chain C: 12 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-5 | 3 | 11 |
| β-strand | 9-12 | 4 | 12 |
| β-strand | 18-25 | 8 | 11 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 12 |
| β-strand | 45-52 | 8 | 12 |
| β-strand | 57-60 | 4 | 12 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 11 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 11 |
| α-helix | 84 | 1 | |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 12 |
| β-strand | 104-105 | 2 | 12 |
| β-strand | 109-113 | 5 | 12 |
| α-helix | 116-118 | 3 | |
| β-strand | 119 | 1 | 13 |
| α-helix | 120-121 | 2 | |
| β-strand | 122-126 | 5 | 14 |
| α-helix | 127-129 | 3 | |
| β-strand | 137-147 | 11 | 14 |
| β-strand | 148 | 1 | 13 |
| β-strand | 153-156 | 4 | 15 |
| α-helix | 157-159 | 3 | |
| β-strand | 161 | 1 | 15 |
| β-strand | 165-167 | 3 | 14 |
| α-helix | 168-170 | 3 | |
| β-strand | 171-172 | 2 | 14 |
| β-strand | 178-187 | 10 | 14 |
| α-helix | 188-190 | 3 | |
| β-strand | 191 | 1 | 16 |
| β-strand | 194 | 1 | 16 |
| β-strand | 197-202 | 6 | 15 |
| β-strand | 207-212 | 6 | 15 |
| α-helix | 215-217 | 3 | |
Chain D: 8 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 17 |
| β-strand | 10-13 | 4 | 18 |
| β-strand | 19-25 | 7 | 17 |
| β-strand | 33-38 | 6 | 18 |
| β-strand | 44-49 | 6 | 18 |
| β-strand | 53-54 | 2 | 18 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 17 |
| β-strand | 70-75 | 6 | 17 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 18 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 18 |
| β-strand | 102-106 | 5 | 18 |
| β-strand | 111 | 1 | 19 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 20 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 20 |
| β-strand | 140 | 1 | 19 |
| β-strand | 145-150 | 6 | 21 |
| β-strand | 153-154 | 2 | 21 |
| β-strand | 159-163 | 5 | 20 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 20 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 21 |
| β-strand | 205-210 | 6 | 21 |
Chain E: 8 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 544-546 | 3 | |
| β-strand | 550-555 | 6 | 22 |
| β-strand | 558-562 | 5 | 22 |
| α-helix | 564-567 | 4 | |
| β-strand | 575-582 | 8 | 23 |
| β-strand | 588-594 | 7 | 23 |
| β-strand | 599-602 | 4 | 22 |
| β-strand | 610-618 | 9 | 23 |
| α-helix | 623-628 | 6 | |
| β-strand | 629-632 | 4 | 23 |
| α-helix | 633-635 | 3 | |
| α-helix | 638-642 | 5 | |
| β-strand | 643-648 | 6 | 24 |
| β-strand | 655-660 | 6 | 24 |
| β-strand | 669-676 | 8 | 25 |
| β-strand | 683-689 | 7 | 25 |
| β-strand | 696-699 | 4 | 24 |
| α-helix | 702-703 | 2 | |
| β-strand | 707-715 | 9 | 25 |
| β-strand | 720 | 1 | 25 |
| α-helix | 725-726 | 2 | |
| β-strand | 727-730 | 4 | 25 |
| α-helix | 731-734 | 4 | |
Chain F: 8 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 541-546 | 6 | |
| β-strand | 550-555 | 6 | 26 |
| β-strand | 558-562 | 5 | 26 |
| β-strand | 575-582 | 8 | 27 |
| β-strand | 588-594 | 7 | 27 |
| β-strand | 599-602 | 4 | 26 |
| β-strand | 610-618 | 9 | 27 |
| α-helix | 622-628 | 7 | |
| β-strand | 629-632 | 4 | 27 |
| α-helix | 633-635 | 3 | |
| α-helix | 638-642 | 5 | |
| β-strand | 643-648 | 6 | 28 |
| β-strand | 655-660 | 6 | 28 |
| β-strand | 669-676 | 8 | 25 |
| β-strand | 683-689 | 7 | 25 |
| β-strand | 696-699 | 4 | 28 |
| α-helix | 702-703 | 2 | |
| β-strand | 707-715 | 9 | 25 |
| β-strand | 720 | 1 | 25 |
| α-helix | 721-723 | 3 | |
| α-helix | 725-726 | 2 | |
| β-strand | 727-730 | 4 | 25 |
| α-helix | 731-734 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| the chimeric Fab fragment of 3H7 (heavy chain) | A, C | protein | 227 | Homo sapiens | |
| the chimeric Fab fragment of 3H7 (light chain) | B, D | protein | 214 | Homo sapiens | |
| Angiopoietin-1 receptor | E, F | protein | 199 | Homo sapiens | Q02763 (AlphaFold model) |
Sequence of entity 1 (A, C), FASTA
>7E72_1 the chimeric Fab fragment of 3H7 (heavy chain) (chains A, C)
QVQLQQPGAELVRPGASVKLSCKASGYSFTSYWMNWVKQRPGQGLEWIGMIHPSDSETRL
NQKFMDKATLTVDKSSSTAYMQLSSPTSEDSAVYYCARGLYGNSWGQGTLVTVSAASTKG
PSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSL
SSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHH
Sequence of entity 2 (B, D), FASTA
>7E72_2 the chimeric Fab fragment of 3H7 (light chain) (chains B, D)
DIQMTQSPSSLSASLGERVSLTCRASQDIGISLNWLQQEPDGTIKRLIYATSSLDSGVPK
RFSGSRSGSDYSLTISSLESEDFVDYYCLQYASSPYTFGGGTKLEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 3 (E, F), FASTA
>7E72_3 Angiopoietin-1 receptor (chains E, F)
GSHMIGLPPPRGLNLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQKSDQQNIKVPGN
LTSVLLNNLHPREQYVVRARVNTKAQGEWSEDLTAWTLSDILPPQPENIKISNITHSSAV
ISWTILDGYSISSITIRYKVQGKNEDQHVDVKIKNATITQYQLKGLEPETAYQVDIFAEN
NIGSSNPAFSHELVTLPES
Primary citation
Structural insights into the clustering and activation of Tie2 receptor mediated by Tie2 agonistic antibody. Jo, G., Bae, J., Hong, H.J. et al. Nat Commun (2021) 12:6287-6287. DOI 10.1038/s41467-021-26620-1 · 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
- 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
Browse structure collections
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