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The crystal structure of oxidoreductase from sinorhizobium meliloti
Analyse The crystal structure of oxidoreductase from sinorhizobium meliloti in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V5N
- Type
- protein
- Length
- 1,413 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxidoreductase
- EC
- 1.1.1.-
- UniProt
- Q92LX1
- Pockets
- 14 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxidoreductase (EC 1.1.1.-) | protein | 356 | 37% helix, 24% strand | Q92LX1 |
| B | Oxidoreductase (EC 1.1.1.-) | protein | 355 | 37% helix, 24% strand | Q92LX1 |
| C | Oxidoreductase (EC 1.1.1.-) | protein | 352 | 38% helix, 24% strand | Q92LX1 |
| D | Oxidoreductase (EC 1.1.1.-) | protein | 350 | 38% helix, 24% strand | Q92LX1 |
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1115 | 0.87 | 0.88 | 138 | empty |
| 2 | 496 | 0.69 | 0.80 | 69 | empty |
| 3 | 343 | 0.64 | 0.80 | 53 | empty |
| 4 | 205 | 0.62 | 0.82 | 28 | empty |
| 5 | 332 | 0.60 | 0.77 | 47 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1843 Ų buried · 39 hydrogen bonds · protein-protein
- C–D · 1793 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1380 Ų buried · 25 hydrogen bonds · protein-protein
- A–D · 1361 Ų buried · 23 hydrogen bonds · protein-protein
- B–D · 384 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 40 modified (engineered).
Compared structures
- 3V5N · The crystal structure of oxidoreductase from Sinorhizobium meliloti · 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 Q92LX1
- Elsewhere: RCSB PDB 3V5N · PDBe 3V5N · UniProt Q92LX1
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