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NMR spatial structure of the trimeric mutant tm domain of VEGFR2 receptor.

Analyse NMR spatial structure of the trimeric mutant tm domain of VEGFR2 receptor. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2MET
Type
protein
Length
111 residues
Chains
3
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Vascular endothelial growth factor receptor 2
EC
2.7.10.1
UniProt
P35968
Pockets
1 · best druggability 0.43

Structure

solution nmr · 1 distinct chain · 81% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CVascular endothelial growth factor receptor 2 (EC 2.7.10.1)protein3781% helix, 0% strandP35968

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11290.430.7516empty

Interfaces

3 interfaces between chains.

  • B–C · 342 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 339 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 336 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 2MET · NMR spatial structure of the trimeric mutant TM domain of VEGFR2 receptor. · the same entry in another collection · chain C against C, TM-score 1.00
  • P35968 · AlphaFold monomer V2.0 prediction for vascular endothelial growth factor receptor 2… · a predicted model of the same protein · chain A against A, TM-score 0.56

Analyse

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