Research workbench
Carboxylic ester hydrolase, C 2 2 21 space group
Analyse Carboxylic ester hydrolase, C 2 2 21 space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LE7
- Type
- protein
- Length
- 246 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Group X secretory phospholipase A2
- EC
- 3.1.1.4
- UniProt
- O15496
- Ligands
- CA
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Group X secretory phospholipase A2 (EC 3.1.1.4) | protein | 123 | 46% helix, 9% strand | O15496 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.62 | 0.80 | 27 | CA, MPD |
| 2 | 210 | 0.56 | 0.79 | 22 | MPD |
| 3 | 89 | 0.42 | 0.79 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 447 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
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 O15496
- Elsewhere: RCSB PDB 1LE7 · PDBe 1LE7 · UniProt O15496
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