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Structure of the transforming growth factor-beta neutralizing antibody gc-1008

Analyse Structure of the transforming growth factor-beta neutralizing antibody gc-1008 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EO0
Type
protein
Length
870 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gc-1008 Fab light chain; Gc-1008 Fab heavy chain
Pockets
9 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CGc-1008 Fab light chainprotein2157% helix, 50% strand—
B, DGc-1008 Fab heavy chainprotein2207% helix, 51% strand—

Ligands and binding sites

  • GOL · Glycerol · additive · 6 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17080.730.7970empty
24730.620.7658empty
34410.590.7548empty
4590.480.8518empty
51000.390.7624empty

Interfaces

5 interfaces between chains.

  • C–D · 1787 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 1786 Ų buried · 11 hydrogen bonds · protein-protein
  • A–C · 402 Ų buried · 4 hydrogen bonds · protein-protein
  • B–C · 49 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 46 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 3EO0 · Structure of the Transforming Growth Factor-Beta Neutralizing Antibody GC-1008 · the same entry in another collection · chain A against A, TM-score 1.00

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