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PFRH5-binding monoclonal antibody R5.004

Analyse PFRH5-binding monoclonal antibody R5.004 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6RCO
Type
protein
Length
872 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
R5.004 heavy chain; R5.004 light chain
Pockets
6 · best druggability 0.73

Structure

x-ray diffraction · 4 distinct chains · 7% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AR5.004 heavy chainprotein2217% helix, 54% strand—
BR5.004 light chainprotein2147% helix, 51% strand—
CR5.004 heavy chainprotein2228% helix, 54% strand—
DR5.004 light chainprotein2157% helix, 51% strand—

Ligands and binding sites

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111300.730.76100GOL
21780.550.8024empty
31580.480.7734GOL
41560.420.7432GOL
5880.420.7818ACT, GOL

Interfaces

5 interfaces between chains.

  • C–D · 1898 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 1852 Ų buried · 14 hydrogen bonds · protein-protein
  • A–D · 190 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 51 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 28 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 6RCO · PfRH5-binding monoclonal antibody R5.004 · the same entry in another collection · chain A against A, TM-score 1.00

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