Research workbench
X-ray structure of gene product from arabidopsis thaliana AT2G19940
Analyse X-ray structure of gene product from arabidopsis thaliana AT2G19940 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XYG
- Type
- protein
- Length
- 1,380 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative N-acetyl-gamma-glutamyl-phosphate reductase
- UniProt
- Q93Z70
- Pockets
- 17 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Putative N-acetyl-gamma-glutamyl-phosphate reductase | protein | 345 | 35% helix, 21% strand | Q93Z70 |
Pockets
17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.75 | 0.99 | 12 | empty |
| 2 | 62 | 0.74 | 0.99 | 12 | empty |
| 3 | 665 | 0.70 | 0.78 | 74 | empty |
| 4 | 749 | 0.70 | 0.77 | 77 | empty |
| 5 | 667 | 0.70 | 0.78 | 72 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2151 Ų buried · 48 hydrogen bonds · protein-protein
- A–D · 2150 Ų buried · 47 hydrogen bonds · protein-protein
- C–D · 1550 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1543 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 925 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1XYG · X-ray structure of gene product from arabidopsis thaliana AT2G19940 · the same entry in another collection · chain D against D, TM-score 1.00
- Q93Z70 · AlphaFold monomer V2.0 prediction for probable N-acetyl-gamma- glutamyl-phosphate… · a predicted model of the same protein · chain D 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 Q93Z70
- Elsewhere: RCSB PDB 1XYG · PDBe 1XYG · UniProt Q93Z70
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