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The crystal structure of lysophospholipid acyltransferase LPCAT3 (MOBAT5) in its monomeric and apo form
Analyse The crystal structure of lysophospholipid acyltransferase LPCAT3 (MOBAT5) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EWT
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysophospholipid acyltransferase 5
- UniProt
- A0A1L1RNG8
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysophospholipid acyltransferase 5 | protein | 417 | 63% helix, 1% strand | A0A1L1RNG8 |
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 | 957 | 0.84 | 0.85 | 83 | empty |
| 2 | 204 | 0.61 | 0.81 | 31 | empty |
| 3 | 130 | 0.57 | 0.84 | 23 | empty |
| 4 | 90 | 0.46 | 0.80 | 14 | empty |
Compared structures
- 7EWT · The crystal structure of Lysophospholipid acyltransferase LPCAT3 (MOBAT5) in its… · 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 A0A1L1RNG8
- Elsewhere: RCSB PDB 7EWT · PDBe 7EWT · UniProt A0A1L1RNG8
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