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MolNFT v1 · #165823 · protein

Cryo-EM structure of helical lipoprotein lipase

6U7M: “Cryo-EM structure of helical lipoprotein lipase”. Electron microscopy, 20 pockets (best druggability 0.75). MolNFT v1 #165823 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6U7M
Type
protein
Length
12,510 residues
Chains
30
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lipoprotein lipase
EC
3.1.1.34
UniProt
P11151
Pockets
20 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 16% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, a, b, c, d, e, f, g, h, iLipoprotein lipase (EC 3.1.1.34)protein41716% helix, 26% strandP11151

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19520.750.78107empty
2520.730.9916empty
3530.730.9816empty
4510.720.9816empty
5530.720.9815empty

Interfaces

46 interfaces between chains.

  • I–h · 1270 Ų buried · 0 hydrogen bonds · protein-protein
  • D–e · 1266 Ų buried · 0 hydrogen bonds · protein-protein
  • C–b · 1262 Ų buried · 0 hydrogen bonds · protein-protein
  • G–f · 1253 Ų buried · 0 hydrogen bonds · protein-protein
  • A–a · 1251 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 150 disulfide (disulfide).

Compared structures

  • 6U7M · Cryo-EM Structure of Helical Lipoprotein Lipase · the same entry in another collection · chain A against A, TM-score 1.00

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