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Structure of rvfv gn and human monoclonal antibody R12

Analyse Structure of rvfv gn and human monoclonal antibody R12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IEK
Type
protein
Length
1,484 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nsmgngc; Heavy chain of Fab R12; Light chain of Fab R12
UniProt
H9BSP3
Pockets
18 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 9% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DNsmgngcprotein30114% helix, 31% strandH9BSP3
B, EHeavy chain of Fab R12protein2234% helix, 48% strand—
C, FLight chain of Fab R12protein2188% helix, 48% strand—

Pockets

18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18560.750.7983empty
27880.750.8092empty
310630.710.7593empty
41510.670.8828empty
56290.640.7457empty

Interfaces

9 interfaces between chains.

  • B–C · 1893 Ų buried · 10 hydrogen bonds · protein-protein
  • E–F · 1850 Ų buried · 8 hydrogen bonds · protein-protein
  • A–F · 452 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 435 Ų buried · 9 hydrogen bonds · protein-protein
  • D–F · 415 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 26 disulfide (disulfide).

Compared structures

  • 6IEK · Structure of RVFV Gn and human monoclonal antibody R12 · the same entry in another collection · chain A against A, TM-score 1.00

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