Research workbench
Structure of the apo form of the no response regulator nsrr
Analyse Structure of the apo form of the no response regulator nsrr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N08
- Type
- protein
- Length
- 635 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional repressor nsrr
- UniProt
- Q9L132
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 65% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Hth-type transcriptional repressor nsrr | protein | 127 | 65% helix, 3% strand | Q9L132 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 892 | 0.82 | 0.84 | 100 | empty |
| 2 | 967 | 0.81 | 0.82 | 94 | empty |
| 3 | 509 | 0.70 | 0.80 | 65 | empty |
| 4 | 263 | 0.68 | 0.83 | 43 | empty |
Interfaces
7 interfaces between chains.
- C–E · 1261 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 1256 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 831 Ų buried · 7 hydrogen bonds · protein-protein
- B–E · 716 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 161 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5N08 · Structure of the apo form of the NO response regulator NsrR · the same entry in another collection · chain A against A, TM-score 1.00
- Q9L132 · AlphaFold monomer V2.0 prediction for hth-type transcriptional repressor nsrr (Q9L132) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 Q9L132
- Elsewhere: RCSB PDB 5N08 · PDBe 5N08 · UniProt Q9L132
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