Research workbench
Crystal structure of putative N-acetyl-gamma-glutamyl- phosphate reductase (AK071544) from rice (oryza sativa)
Analyse Crystal structure of putative N-acetyl-gamma-glutamyl- phosphate reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CVO
- Type
- protein
- Length
- 1,389 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative semialdehyde dehydrogenase
- EC
- 1.2.1.38
- UniProt
- Q6AV34
- Pockets
- 12 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Putative semialdehyde dehydrogenase (EC 1.2.1.38) | protein | 348 | 35% helix, 21% strand | Q6AV34 |
| D | Putative semialdehyde dehydrogenase (EC 1.2.1.38) | protein | 345 | 35% helix, 21% strand | Q6AV34 |
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.78 | 0.99 | 17 | empty |
| 2 | 89 | 0.78 | 0.99 | 16 | empty |
| 3 | 599 | 0.69 | 0.78 | 85 | empty |
| 4 | 593 | 0.68 | 0.77 | 76 | empty |
| 5 | 542 | 0.68 | 0.78 | 50 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2177 Ų buried · 35 hydrogen bonds · protein-protein
- A–B · 2173 Ų buried · 36 hydrogen bonds · protein-protein
- A–D · 1550 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 1544 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 942 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (oxidation).
Compared structures
- 2CVO · Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from… · the same entry in another collection · chain D against D, TM-score 1.00
- Q6AV34 · 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 Q6AV34
- Elsewhere: RCSB PDB 2CVO · PDBe 2CVO · UniProt Q6AV34
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