MolNFT v1 · #155570 · protein
Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana
6LBP · Amidophosphoribosyltransferase 2, chloroplastic: “Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana”. X-ray diffraction, 1 ligand (SF4), 4 pockets (best druggability 0.81). MolNFT v1…
- PDB
- 6LBP
- Type
- protein
- Length
- 920 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amidophosphoribosyltransferase 2, chloroplastic
- EC
- 2.4.2.14
- UniProt
- Q9STG9
- Ligands
- SF4
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Amidophosphoribosyltransferase 2, chloroplastic (EC 2.4.2.14) | protein | 460 | 32% helix, 26% strand | Q9STG9 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1020 | 0.81 | 0.82 | 112 | SF4 |
| 2 | 1071 | 0.81 | 0.82 | 112 | SF4 |
| 3 | 382 | 0.62 | 0.78 | 47 | empty |
| 4 | 89 | 0.40 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2221 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 6LBP · Structure of the Glutamine Phosphoribosylpyrophosphate Amidotransferase from Arabidopsis… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9STG9 · AlphaFold monomer V2.0 prediction for amidophosphoribosyltransferase 2, chloroplastic… · a predicted model of the same protein · chain A 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 Q9STG9
- Elsewhere: RCSB PDB 6LBP · PDBe 6LBP · UniProt Q9STG9
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