MolNFT v1 · #22321 · protein
Crystal structure of the reductoisomerase complexed with a bisphosphonate
1T1S · 1-deoxy-D-xylulose 5-phosphate reductoisomerase: “Crystal structure of the reductoisomerase complexed with a bisphosphonate”. X-ray diffraction, 3 ligands (CBQ, MG, SO4), 4 pockets (best druggability 0.74). MolNFT v1 #22321 on…
- PDB
- 1T1S
- Type
- protein
- Length
- 796 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- EC
- 1.1.1.267
- UniProt
- P45568
- Ligands
- CBQ, MG, SO4
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 1-deoxy-D-xylulose 5-phosphate reductoisomerase (EC 1.1.1.267) | protein | 398 | 49% helix, 15% strand | P45568 |
Ligands and binding sites
- CBQ · [(5-chloro-pyridin-2-ylamino)-phosphono-methyl]-phosphonic acid · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 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 | 240 | 0.74 | 0.89 | 36 | empty |
| 2 | 526 | 0.72 | 0.81 | 73 | SO4, CBQ |
| 3 | 493 | 0.72 | 0.81 | 62 | SO4, CBQ |
| 4 | 53 | 0.30 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1658 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 1T1S · Crystal Structure of the Reductoisomerase Complexed with a Bisphosphonate · the same entry in another collection · chain A against A, TM-score 1.00
- P45568 · AlphaFold monomer V2.0 prediction for 1-deoxy-D-xylulose 5-phosphate reductoisomerase… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P45568
- Elsewhere: RCSB PDB 1T1S · PDBe 1T1S · UniProt P45568
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