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Cryo-EM structure of human TMEM45A

Analyse Cryo-EM structure of human TMEM45A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OQZ
Type
protein
Length
948 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transmembrane protein 45A
UniProt
Q9NWC5
Ligands
PC1
Pockets
18 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 79% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DTransmembrane protein 45Aprotein23779% helix, 0% strandQ9NWC5

Ligands and binding sites

  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · 16 copies · chains A, B, D, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15360.800.8551PC1
22070.760.9033empty
32110.760.9035empty
42190.750.8936empty
52280.750.8935empty

Interfaces

4 interfaces between chains.

  • B–C · 1184 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 1169 Ų buried · 2 hydrogen bonds · protein-protein
  • C–D · 1157 Ų buried · 1 hydrogen bond · protein-protein
  • A–D · 1156 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 7OQZ · Cryo-EM structure of human TMEM45A · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NWC5 · AlphaFold monomer V2.0 prediction for transmembrane protein 45A (Q9NWC5) · a predicted model of the same protein · chain A against A, TM-score 0.96

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