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Apo APH(2")-iva form III

Analyse Apo APH(2")-iva form III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3N4V
Type
protein
Length
596 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
APH(2'')-id
UniProt
O68183
Pockets
6 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAPH(2'')-idprotein29847% helix, 15% strandO68183

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19850.770.7976empty
210590.760.7881empty
3700.330.7514empty
4960.300.7218empty
5730.290.7319empty

Interfaces

1 interface between chains.

  • A–B · 165 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3N4V · apo APH(2)-IVa form III" · the same entry in another collection · chain A against A, TM-score 1.00

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