Research workbench
Cryo-EM structure of helical lipoprotein lipase
Analyse Cryo-EM structure of helical lipoprotein lipase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 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, i | Lipoprotein lipase (EC 3.1.1.34) | protein | 417 | 16% helix, 26% strand | P11151 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 952 | 0.75 | 0.78 | 107 | empty |
| 2 | 52 | 0.73 | 0.99 | 16 | empty |
| 3 | 53 | 0.73 | 0.98 | 16 | empty |
| 4 | 51 | 0.72 | 0.98 | 16 | empty |
| 5 | 53 | 0.72 | 0.98 | 15 | empty |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P11151
- Elsewhere: RCSB PDB 6U7M · PDBe 6U7M · UniProt P11151
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