MolNFT v1 · #12979 · protein
The crystal structure of glutamine amidotransferase from thermotoga maritima
1KXJ · Amidotransferase hish: “The crystal structure of glutamine amidotransferase from thermotoga maritima”. X-ray diffraction, 1 ligand (PO4), 3 pockets (best druggability 0.59). MolNFT v1 #12979 on GenesisL1: 3D structure, binding sites…
- PDB
- 1KXJ
- Type
- protein
- Length
- 404 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amidotransferase hish
- EC
- 2.4.2.-
- UniProt
- Q9X0C8
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amidotransferase hish (EC 2.4.2.-) | protein | 203 | 26% helix, 33% strand | Q9X0C8 |
| B | Amidotransferase hish (EC 2.4.2.-) | protein | 201 | 28% helix, 35% strand | Q9X0C8 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 277 | 0.59 | 0.78 | 39 | empty |
| 2 | 67 | 0.45 | 0.82 | 15 | PO4 |
| 3 | 60 | 0.42 | 0.82 | 15 | PO4 |
Interfaces
1 interface between chains.
- A–B · 662 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1KXJ · The Crystal Structure of Glutamine Amidotransferase from Thermotoga maritima · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X0C8 · AlphaFold monomer V2.0 prediction for imidazole glycerol phosphate synthase subunit hish… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q9X0C8
- Elsewhere: RCSB PDB 1KXJ · PDBe 1KXJ · UniProt Q9X0C8
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