Research workbench
Crystal structure of polyneuridine aldehyde esterase mutant (H244A)
Analyse Crystal structure of polyneuridine aldehyde esterase mutant (H244A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WFM
- Type
- protein
- Length
- 1,275 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyneuridine aldehyde esterase
- EC
- 3.1.1.78
- UniProt
- Q9SE93
- Pockets
- 11 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Polyneuridine aldehyde esterase (EC 3.1.1.78) | protein | 255 | 40% helix, 19% strand | Q9SE93 |
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 359 | 0.78 | 0.87 | 48 | empty |
| 2 | 397 | 0.77 | 0.86 | 61 | empty |
| 3 | 304 | 0.75 | 0.87 | 36 | empty |
| 4 | 300 | 0.74 | 0.86 | 37 | empty |
| 5 | 297 | 0.70 | 0.84 | 38 | empty |
Interfaces
4 interfaces between chains.
- C–E · 941 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 921 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 792 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 479 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 2WFM · Crystal structure of polyneuridine aldehyde esterase mutant (H244A) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9SE93 · AlphaFold monomer V2.0 prediction for polyneuridine-aldehyde esterase (Q9SE93) · a predicted model of the same protein · 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 Q9SE93
- Elsewhere: RCSB PDB 2WFM · PDBe 2WFM · UniProt Q9SE93
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