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Cryo-EM structure of ATP-bound human very long-chain fatty acid ABC transporter ABCD1

Analyse Cryo-EM structure of ATP-bound human very long-chain fatty acid ABC transporter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VX8
Type
protein
Length
1,120 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peroxisomal membrane protein RELATED,ATP-binding cassette sub-family D member 1
EC
3.1.2.-, 7.6.2.-
UniProt
P33897
Ligands
ATP, MG
Pockets
14 · best druggability 0.87

Structure

electron microscopy · 1 distinct chain · 58% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, APeroxisomal membrane protein RELATED,ATP-binding cassette sub-family D member 1 (EC 3.1.2.-, 7.6.2.-)protein56058% helix, 8% strandP33897

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains B, A
  • MG · Magnesium ion · metal · 2 copies · chains B, A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111690.870.89142ATP, MG
211900.720.7691empty
35560.660.7758empty
44930.640.7649empty
52580.540.7645empty

Interfaces

1 interface between chains.

  • B–A · 6378 Ų buried · 46 hydrogen bonds · protein-protein

Compared structures

  • 7VX8 · Cryo-EM structure of ATP-bound human very long-chain fatty acid ABC transporter ABCD1 · the same entry in another collection · chain B against B, TM-score 1.00
  • P33897 · AlphaFold monomer V2.0 prediction for ATP-binding cassette sub-family D member 1 (P33897) · a predicted model of the same protein · chain B against A, TM-score 0.92

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