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Crystal structure of polyneuridine aldehyde esterase
Analyse Crystal structure of polyneuridine aldehyde esterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WFL
- Type
- protein
- Length
- 510 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyneuridine-aldehyde esterase
- EC
- 3.1.1.78
- UniProt
- Q9SE93
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Polyneuridine-aldehyde esterase (EC 3.1.1.78) | protein | 255 | 40% helix, 18% strand | Q9SE93 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 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 | 390 | 0.73 | 0.84 | 48 | SO4 |
| 2 | 287 | 0.72 | 0.85 | 36 | SO4 |
| 3 | 163 | 0.46 | 0.76 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 879 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (artifact).
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 Q9SE93
- Elsewhere: RCSB PDB 2WFL · PDBe 2WFL · UniProt Q9SE93
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