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Structure of a human a-type potassium channel accelerating factor dppx, a member of the dipeptidyl aminopeptidase family

Analyse Structure of a human a-type potassium channel accelerating factor dppx, a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1XFD
Type
protein
Length
2,892 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dipeptidyl aminopeptidase-like protein 6
Ligands
NAG, BMA, MAN, NDG
Pockets
20 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DDipeptidyl aminopeptidase-like protein 6protein72314% helix, 31% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 40 copies · chains A, B, C, D
  • BMA · beta-D-mannopyranose · sugar · 12 copies · chains A, D
  • MAN · alpha-D-mannopyranose · sugar · 7 copies · chains B, D
  • NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 4 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19010.760.79115empty
27180.750.8084empty
36460.750.8182empty
46490.750.8183empty
55220.670.7839empty

Interfaces

2 interfaces between chains.

  • A–B · 1676 Ų buried · 26 hydrogen bonds · protein-protein
  • C–D · 1665 Ų buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 22 glycan, 16 disulfide (N-glycosylation, disulfide).

Compared structures

  • 1XFD · Structure of a human A-type Potassium Channel Accelerating factor DPPX, a member of the… · the same entry in another collection · chain C against C, TM-score 1.00

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