Research workbench
Cryo-EM structure of the (TGA3)2-(NPR1)2-(TGA3)2 complex
Analyse Cryo-EM structure of the (TGA3)2-(NPR1)2-(TGA3)2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TAC
- Type
- protein
- Length
- 1,526 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulatory protein NPR1; Transcription factor TGA3
- UniProt
- P93002, Q39234
- Ligands
- PLM, ZN
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 3 distinct chains · 74% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Regulatory protein NPR1 | protein | 347 | 62% helix, 4% strand | P93002 |
| C, E | Transcription factor TGA3 | protein | 209 | 85% helix, 1% strand | Q39234 |
| D, F | Transcription factor TGA3 | protein | 207 | 84% helix, 1% strand | Q39234 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 4 copies · chains C, D, E, F
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 511 | 0.85 | 0.91 | 55 | PLM |
| 2 | 364 | 0.84 | 0.93 | 42 | PLM |
| 3 | 429 | 0.83 | 0.91 | 49 | PLM |
| 4 | 400 | 0.83 | 0.91 | 50 | PLM |
| 5 | 869 | 0.78 | 0.80 | 65 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1306 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 1281 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 1194 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 611 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 597 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7TAC · Cryo-EM structure of the (TGA3)2-(NPR1)2-(TGA3)2 complex · the same entry in another collection · chain F against F, TM-score 1.00
- P93002 · AlphaFold monomer V2.0 prediction for regulatory protein NPR1 (P93002) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q39234 · AlphaFold monomer V2.0 prediction for transcription factor TGA3 (Q39234) · a predicted model of the same protein · chain C 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 P93002
- Every structure of UniProt Q39234
- Elsewhere: RCSB PDB 7TAC · PDBe 7TAC · UniProt P93002 · UniProt Q39234
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