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MolNFT v1 · #164351 · protein

Human prion protein (prp) fragment 119-231 (G127V V129 variant) complexed to icsm 18 (anti-prp therapeutic antibody) Fab fragment

6SUZ · Major prion protein: “Human prion protein (prp) fragment 119-231 (G127V V129 variant) complexed to icsm 18 (anti-prp therapeutic…”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.59). MolNFT v1 #164351 on…

PDB
6SUZ
Type
protein
Length
525 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major prion protein; Icsm 18-anti-prp therapeutic Fab heavy chain; Icsm 18-anti-prp…
UniProt
P04156
Ligands
SO4
Pockets
4 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 16% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMajor prion proteinprotein9960% helix, 4% strandP04156
HIcsm 18-anti-prp therapeutic Fab heavy chainprotein2157% helix, 54% strand—
LIcsm 18-anti-prp therapeutic Fab light chainprotein2116% helix, 54% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14640.590.7460empty
21620.460.7627empty
3660.320.7515empty
4610.300.7515empty

Interfaces

3 interfaces between chains.

  • H–L · 1630 Ų buried · 14 hydrogen bonds · protein-protein
  • A–H · 581 Ų buried · 11 hydrogen bonds · protein-protein
  • A–L · 384 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 6SUZ · Human prion protein (PrP) fragment 119-231 (G127V V129 variant) complexed to ICSM 18… · the same entry in another collection · chain A against A, TM-score 1.00

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