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Structure of ATATM3 in the inward-facing conformation

Analyse Structure of ATATM3 in the inward-facing conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7N58
Type
protein
Length
1,200 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ABC transporter B family member 25, mitochondrial
UniProt
Q9LVM1
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 60% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BABC transporter B family member 25, mitochondrialprotein60060% helix, 9% strandQ9LVM1

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110000.820.8382empty
29440.770.7976empty
31530.730.9124empty
42000.720.8939empty
52990.710.8436empty

Interfaces

1 interface between chains.

  • A–B · 4824 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

  • 7N58 · Structure of AtAtm3 in the inward-facing conformation · the same entry in another collection · chain B against B, TM-score 1.00
  • Q9LVM1 · AlphaFold monomer V2.0 prediction for ABC transporter B family member 25, mitochondrial… · a predicted model of the same protein · chain B against A, TM-score 0.91

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