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Structure of the G6 Fab, a phage derived VEGF binding Fab

Analyse Structure of the G6 Fab, a phage derived VEGF binding Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FJF
Type
protein
Length
5,148 residues
Chains
24
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Light chain of a VEGF binding antibody; Heavy chain of a VEGF binding antibody
UniProt
Q6GMX8, Q569F4
Pockets
20 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
L, A, C, E, G, J, M, O, Q, S, U, WLight chain of a VEGF binding antibodyprotein2116% helix, 50% strandQ6GMX8
H, B, D, F, I, K, N, P, R, T, V, XHeavy chain of a VEGF binding antibodyprotein2188% helix, 50% strandQ569F4

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18860.710.76114empty
211910.690.74130empty
37040.680.7697empty
47080.650.7492empty
53500.610.7871empty

Interfaces

56 interfaces between chains.

  • W–X · 1897 Ų buried · 11 hydrogen bonds · protein-protein
  • L–H · 1885 Ų buried · 15 hydrogen bonds · protein-protein
  • M–N · 1869 Ų buried · 16 hydrogen bonds · protein-protein
  • S–T · 1860 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 1840 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 48 disulfide (disulfide).

Compared structures

  • 2FJF · Structure of the G6 Fab, a phage derived VEGF binding Fab · the same entry in another collection · chain L against L, TM-score 1.00

Analyse

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