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Crystal structure of choline oxidase S101A mutant
Analyse Crystal structure of choline oxidase S101A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NNE
- Type
- protein
- Length
- 4,237 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Choline oxidase
- EC
- 1.1.3.17
- UniProt
- Q7X2H8
- Ligands
- FAD
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 3 distinct chains · 26% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F, H | Choline oxidase (EC 1.1.3.17) | protein | 530 | 26% helix, 24% strand | Q7X2H8 |
| C | Choline oxidase (EC 1.1.3.17) | protein | 528 | 26% helix, 24% strand | Q7X2H8 |
| G | Choline oxidase (EC 1.1.3.17) | protein | 529 | 26% helix, 24% strand | Q7X2H8 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- ACT · Acetate ion · additive · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 383 | 0.88 | 0.96 | 64 | FAD, ACT |
| 2 | 372 | 0.88 | 0.96 | 61 | FAD, ACT |
| 3 | 348 | 0.87 | 0.97 | 61 | FAD, ACT |
| 4 | 355 | 0.87 | 0.96 | 61 | FAD, ACT |
| 5 | 372 | 0.87 | 0.96 | 62 | FAD, ACT |
Interfaces
11 interfaces between chains.
- G–H · 1310 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 1265 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 1250 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1232 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 697 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 cofactor (flavinylation).
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 Q7X2H8
- Elsewhere: RCSB PDB 3NNE · PDBe 3NNE · UniProt Q7X2H8
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