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4E10 germline encoded precursor NO.7 in complex with epitope scaffold T117

Analyse 4E10 germline encoded precursor NO.7 in complex with epitope scaffold T117 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ODX
Type
protein
Length
775 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
4E10 epitope scaffold T117; GEP7 fv heavy chain; GEP7 fv light chain
Pockets
6 · best druggability 0.69

Structure

x-ray diffraction · 5 distinct chains · 23% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
X4E10 epitope scaffold T117protein15244% helix, 24% strand—
A, HGEP7 fv heavy chainprotein1272% helix, 52% strand—
BGEP7 fv light chainprotein1076% helix, 52% strand—
LGEP7 fv light chainprotein1096% helix, 53% strand—
Y4E10 epitope scaffold T117protein15344% helix, 24% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17480.690.7674empty
21070.570.8520empty
31150.420.7721empty
4930.400.7719empty
5650.300.7417empty

Interfaces

8 interfaces between chains.

  • B–H · 762 Ų buried · 7 hydrogen bonds · protein-protein
  • A–L · 754 Ų buried · 6 hydrogen bonds · protein-protein
  • A–Y · 734 Ų buried · 5 hydrogen bonds · protein-protein
  • X–H · 721 Ų buried · 4 hydrogen bonds · protein-protein
  • X–B · 224 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 4ODX · 4E10 germline encoded precursor no.7 in complex with epitope scaffold T117 · the same entry in another collection · chain X against X, TM-score 1.00

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