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Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TM1782) from thermotoga maritima at 1.80 a resolution
Analyse Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TM1782) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VKN
- Type
- protein
- Length
- 1,351 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyl-gamma-glutamyl-phosphate reductase
- EC
- 1.2.1.38
- UniProt
- Q9X2A2
- Pockets
- 12 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) | protein | 340 | 36% helix, 23% strand | Q9X2A2 |
| C | N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) | protein | 336 | 36% helix, 23% strand | Q9X2A2 |
| D | N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) | protein | 335 | 35% helix, 23% strand | Q9X2A2 |
Pockets
12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 842 | 0.75 | 0.79 | 81 | empty |
| 2 | 603 | 0.69 | 0.78 | 53 | empty |
| 3 | 65 | 0.69 | 0.96 | 18 | empty |
| 4 | 724 | 0.67 | 0.75 | 81 | empty |
| 5 | 515 | 0.63 | 0.76 | 51 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1914 Ų buried · 40 hydrogen bonds · protein-protein
- A–D · 1908 Ų buried · 35 hydrogen bonds · protein-protein
- B–D · 1397 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 1376 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 875 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 modified (engineered).
Compared structures
- 1VKN · Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TM1782) from Thermotoga… · the same entry in another collection · chain D against D, TM-score 1.00
- Q9X2A2 · AlphaFold monomer V2.0 prediction for N-acetyl-gamma-glutamyl- phosphate reductase… · a predicted model of the same protein · chain C against A, TM-score 0.99
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 Q9X2A2
- Elsewhere: RCSB PDB 1VKN · PDBe 1VKN · UniProt Q9X2A2
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