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HSPEPT2 bound to ala-phe in the inward facing partially occluded conformation

Analyse HSPEPT2 bound to ala-phe in the inward facing partially occluded conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7PMY
Type
protein
Length
659 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Solute carrier family 15 member 2; Ala-phe
UniProt
Q16348
Pockets
7 · best druggability 0.76

Structure

electron microscopy · 2 distinct chains · 56% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASolute carrier family 15 member 2protein65756% helix, 18% strandQ16348
BAla-pheprotein20% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1830.760.9922empty
23660.760.8641empty
36710.750.8174empty
42190.520.7620empty
51700.480.7626empty

Interfaces

1 interface between chains.

  • A–B · 297 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 7PMY · HsPepT2 bound to Ala-Phe in the inward facing partially occluded conformation · the same entry in another collection · chain A against A, TM-score 1.00
  • Q16348 · AlphaFold monomer V2.0 prediction for solute carrier family 15 member 2 (Q16348) · a predicted model of the same protein · chain A against A, TM-score 0.93

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