Research workbench
Crystal structure of gamma-glutamyl phosphate reductase (YOR323C) from saccharomyces cerevisiae at 2.40 a resolution
Analyse Crystal structure of gamma-glutamyl phosphate reductase (YOR323C) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VLU
- Type
- protein
- Length
- 792 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-glutamyl phosphate reductase
- EC
- 1.2.1.41
- UniProt
- P54885
- Ligands
- CL
- Pockets
- 4 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-glutamyl phosphate reductase (EC 1.2.1.41) | protein | 395 | 47% helix, 18% strand | P54885 |
| B | Gamma-glutamyl phosphate reductase (EC 1.2.1.41) | protein | 397 | 46% helix, 19% strand | P54885 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 135 | 0.44 | 0.76 | 24 | empty |
| 2 | 70 | 0.36 | 0.78 | 19 | empty |
| 3 | 82 | 0.36 | 0.76 | 20 | empty |
| 4 | 89 | 0.35 | 0.75 | 22 | empty |
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 1VLU · Crystal structure of Gamma-glutamyl phosphate reductase (yor323c) from Saccharomyces… · the same entry in another collection · chain A against A, TM-score 1.00
- P54885 · AlphaFold monomer V2.0 prediction for gamma-glutamyl phosphate reductase (P54885) · a predicted model of the same protein · chain A against A, TM-score 0.64
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 P54885
- Elsewhere: RCSB PDB 1VLU · PDBe 1VLU · UniProt P54885
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