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MolNFT v1 · #146783 · protein

Cryo EM structure of human seipin

6DS5: “Cryo EM structure of human seipin”. Electron microscopy, 1 ligand (NAG), 20 pockets (best druggability 0.76). MolNFT v1 #146783 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6DS5
Type
protein
Length
1,760 residues
Chains
11
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Seipin
UniProt
Q96G97
Ligands
NAG
Pockets
20 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 14% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, KSeipinprotein16014% helix, 33% strandQ96G97

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 22 copies · chains A, B, C, D, E, F, G, H, I, J, K

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11080.760.9525empty
21020.760.9619empty
31030.760.9619empty
41040.750.9620empty
51030.750.9519empty

Interfaces

11 interfaces between chains.

  • C–D · 1155 Ų buried · 8 hydrogen bonds · protein-protein
  • G–H · 1155 Ų buried · 8 hydrogen bonds · protein-protein
  • D–E · 1154 Ų buried · 8 hydrogen bonds · protein-protein
  • H–I · 1151 Ų buried · 8 hydrogen bonds · protein-protein
  • E–F · 1151 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 disulfide, 11 glycan (disulfide, N-glycosylation).

Compared structures

  • 6DS5 · Cryo EM structure of human SEIPIN · the same entry in another collection · chain K against K, TM-score 1.00
  • Q96G97 · AlphaFold monomer V2.0 prediction for seipin (Q96G97) · a predicted model of the same protein · chain A against A, TM-score 0.95

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