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MolNFT v1 · #152331 · protein

Structure of rvfv gn and human monoclonal antibody R15

6IEB · R15 H chain: “Structure of rvfv gn and human monoclonal antibody R15”. X-ray diffraction, 20 pockets (best druggability 0.58). MolNFT v1 #152331 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6IEB
Type
protein
Length
1,392 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
R15 H chain; R15 L chain; Nsmgngc
UniProt
H9BSP3
Pockets
20 · best druggability 0.58

Structure

x-ray diffraction · 6 distinct chains · 9% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HR15 H chainprotein2118% helix, 49% strand—
LR15 L chainprotein2078% helix, 49% strand—
BNsmgngcprotein29312% helix, 30% strandH9BSP3
ANsmgngcprotein29511% helix, 30% strandH9BSP3
ER15 H chainprotein1823% helix, 51% strand—
FR15 L chainprotein2046% helix, 48% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14580.580.7458empty
24520.570.7450empty
3630.560.8817empty
42330.530.7636empty
51280.520.8120empty

Interfaces

8 interfaces between chains.

  • H–L · 1497 Ų buried · 16 hydrogen bonds · protein-protein
  • E–F · 1319 Ų buried · 15 hydrogen bonds · protein-protein
  • H–A · 493 Ų buried · 4 hydrogen bonds · protein-protein
  • B–E · 437 Ų buried · 4 hydrogen bonds · protein-protein
  • B–F · 314 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 28 disulfide (disulfide).

Compared structures

  • 6IEB · Structure of RVFV Gn and human monoclonal antibody R15 · the same entry in another collection · chain H against H, TM-score 1.00

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