Research workbench
Crystal structure of transcription factor ntca from synechococcus elongatus bound to 2-oxoglutarate
Analyse Crystal structure of transcription factor ntca from synechococcus elongatus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XHK
- Type
- protein
- Length
- 432 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Global nitrogen regulator
- UniProt
- P29283
- Ligands
- AKG
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Global nitrogen regulator | protein | 215 | 41% helix, 27% strand | P29283 |
| B | Global nitrogen regulator | protein | 217 | 43% helix, 26% strand | P29283 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.73 | 0.98 | 20 | empty |
| 2 | 100 | 0.63 | 0.89 | 29 | empty |
| 3 | 228 | 0.53 | 0.77 | 38 | empty |
| 4 | 170 | 0.45 | 0.75 | 25 | empty |
| 5 | 75 | 0.36 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2226 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 2XHK · Crystal structure of transcription factor NtcA from Synechococcus elongatus bound to… · the same entry in another collection · chain A against A, TM-score 1.00
- P29283 · AlphaFold monomer V2.0 prediction for global nitrogen regulator (P29283) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P29283
- Elsewhere: RCSB PDB 2XHK · PDBe 2XHK · UniProt P29283
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