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Structural basis for the function of two anti-VEGF receptor antibodies

Analyse Structural basis for the function of two anti-VEGF receptor antibodies in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3S36
Type
protein
Length
540 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
1121B light chain; 1121B heavy chain; Vascular endothelial growth factor receptor 2
EC
2.7.10.1
UniProt
P35968
Pockets
5 · best druggability 0.54

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
L1121B light chainprotein2146% helix, 48% strand—
H1121B heavy chainprotein2146% helix, 53% strand—
XVascular endothelial growth factor receptor 2 (EC 2.7.10.1)protein1126% helix, 46% strandP35968

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13380.540.7440empty
2590.530.8821empty
31120.460.7930empty
41110.400.7620empty
5500.280.7614empty

Interfaces

3 interfaces between chains.

  • L–H · 1818 Ų buried · 17 hydrogen bonds · protein-protein
  • H–X · 714 Ų buried · 25 hydrogen bonds · protein-protein
  • L–X · 346 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 3S36 · Structural basis for the function of two anti-VEGF receptor antibodies · the same entry in another collection · chain L against L, TM-score 1.00

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