Research workbench
Crystal structure of 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase from Thermus thermophilus HB8
Analyse Crystal structure of 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PX7
- Type
- protein
- Length
- 405 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Thermus thermophilus HB8
- Molecule
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- EC
- 2.7.7.60
- UniProt
- Q5SLX2
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · resolution 2.2 · 2 distinct chains · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60) | protein | 203 | 35% helix, 24% strand | Q5SLX2 |
| B | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60) | protein | 202 | 36% helix, 26% strand | Q5SLX2 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.80 | 0.92 | 41 | empty |
| 2 | 164 | 0.51 | 0.79 | 32 | empty |
| 3 | 148 | 0.48 | 0.78 | 27 | empty |
| 4 | 110 | 0.36 | 0.74 | 25 | empty |
| 5 | 66 | 0.26 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2008 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 2PX7 · Crystal structure of 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5SLX2 · AlphaFold monomer V2.0 prediction for 2-C-methyl-D-erythritol 4-phosphate… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q5SLX2
- Elsewhere: RCSB PDB 2PX7 · PDBe 2PX7 · UniProt Q5SLX2
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