Research workbench
Structure of the hormone-sensitive lipase like ESTD11
Analyse Structure of the hormone-sensitive lipase like ESTD11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AT0
- Type
- protein
- Length
- 589 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ESTD11
- Ligands
- IPH
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ESTD11 | protein | 295 | 44% helix, 17% strand | — |
| B | ESTD11 | protein | 294 | 44% helix, 18% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.79 | 0.92 | 40 | empty |
| 2 | 260 | 0.77 | 0.89 | 39 | FMT |
| 3 | 124 | 0.60 | 0.85 | 25 | empty |
| 4 | 93 | 0.41 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 557 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 7AT0 · Structure of the Hormone-Sensitive Lipase like EstD11 · 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
- Elsewhere: RCSB PDB 7AT0 · PDBe 7AT0
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