MolNFT v1 · #37963 · protein
Crystal structure of glutamyl-TRNA(GLN) amidotransferase subunit a (TM1272) from thermotoga maritima at 1.80 a resolution
2GI3: “Crystal structure of glutamyl-TRNA(GLN) amidotransferase subunit a (TM1272) from thermotoga maritima at 1.80…”. X-ray diffraction, 3 pockets (best druggability 0.69). MolNFT v1 #37963 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2GI3
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamyl-TRNA(GLN) amidotransferase subunit a
- EC
- 6.3.5.-
- UniProt
- Q9X0Z9
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamyl-TRNA(GLN) amidotransferase subunit a (EC 6.3.5.-) | protein | 452 | 39% helix, 17% strand | Q9X0Z9 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.69 | 0.93 | 20 | empty |
| 2 | 212 | 0.64 | 0.83 | 29 | empty |
| 3 | 89 | 0.39 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 11 modified (engineered).
Compared structures
- 2GI3 · Crystal structure of Glutamyl-tRNA(Gln) amidotransferase subunit A (tm1272) from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X0Z9 · AlphaFold monomer V2.0 prediction for glutamyl-TRNA(GLN) amidotransferase subunit a… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q9X0Z9
- Elsewhere: RCSB PDB 2GI3 · PDBe 2GI3 · UniProt Q9X0Z9
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