MolNFT v1 · #8060 · protein
Glutamyl-tRNA reductase from methanopyrus kandleri
1GPJ: “Glutamyl-tRNA reductase from methanopyrus kandleri”. X-ray diffraction, 2 ligands (GLU, GMC), 2 pockets (best druggability 0.56). MolNFT v1 #8060 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1GPJ
- Type
- protein
- Length
- 399 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamyl-tRNA reductase
- EC
- 1.2.1.70
- UniProt
- Q9UXR8
- Ligands
- GLU, GMC
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamyl-tRNA reductase (EC 1.2.1.70) | protein | 399 | 56% helix, 13% strand | Q9UXR8 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · chains A
- GMC · (2R,3R,4S,5S)-4-amino-2-[6-(dimethylamino)-9H-purin-9-yl]-5-(hydroxymethyl)tetrahydro-3-furanol · ligand · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.56 | 0.80 | 24 | empty |
| 2 | 69 | 0.30 | 0.73 | 14 | CIT |
Compared structures
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 Q9UXR8
- Elsewhere: RCSB PDB 1GPJ · PDBe 1GPJ · UniProt Q9UXR8
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