Research workbench
The X-ray structure of CTP:INOSITOL-1-phosphate cytidylyltransferase from archaeoglobus fulgidus
Analyse The X-ray structure of CTP:INOSITOL-1-phosphate cytidylyltransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XME
- Type
- protein
- Length
- 2,407 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CTP-inositol-1-phosphate cytidylyltransferase
- UniProt
- O29976
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 12 distinct chains · 29% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP-inositol-1-phosphate cytidylyltransferase | protein | 201 | 29% helix, 33% strand | O29976 |
| B | CTP-inositol-1-phosphate cytidylyltransferase | protein | 198 | 30% helix, 32% strand | O29976 |
| C | CTP-inositol-1-phosphate cytidylyltransferase | protein | 199 | 28% helix, 32% strand | O29976 |
| D | CTP-inositol-1-phosphate cytidylyltransferase | protein | 201 | 30% helix, 32% strand | O29976 |
| E | CTP-inositol-1-phosphate cytidylyltransferase | protein | 204 | 29% helix, 34% strand | O29976 |
| F | CTP-inositol-1-phosphate cytidylyltransferase | protein | 208 | 28% helix, 32% strand | O29976 |
| G | CTP-inositol-1-phosphate cytidylyltransferase | protein | 199 | 28% helix, 33% strand | O29976 |
| H | CTP-inositol-1-phosphate cytidylyltransferase | protein | 198 | 30% helix, 33% strand | O29976 |
| I | CTP-inositol-1-phosphate cytidylyltransferase | protein | 199 | 27% helix, 31% strand | O29976 |
| J | CTP-inositol-1-phosphate cytidylyltransferase | protein | 200 | 29% helix, 34% strand | O29976 |
| K | CTP-inositol-1-phosphate cytidylyltransferase | protein | 200 | 30% helix, 33% strand | O29976 |
| L | CTP-inositol-1-phosphate cytidylyltransferase | protein | 200 | 28% helix, 31% strand | O29976 |
Ligands and binding sites
- GOL · Glycerol · additive · 8 copies · chains A, B, C, D, E, G, I, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1083 | 0.78 | 0.80 | 110 | empty |
| 2 | 552 | 0.78 | 0.85 | 57 | empty |
| 3 | 808 | 0.77 | 0.81 | 93 | empty |
| 4 | 780 | 0.76 | 0.81 | 88 | empty |
| 5 | 519 | 0.75 | 0.83 | 58 | GOL |
Interfaces
21 interfaces between chains.
- E–F · 1167 Ų buried · 20 hydrogen bonds · protein-protein
- K–L · 1034 Ų buried · 15 hydrogen bonds · protein-protein
- I–J · 1028 Ų buried · 18 hydrogen bonds · protein-protein
- G–H · 953 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 932 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2XME · The X-ray structure of CTP:inositol-1-phosphate cytidylyltransferase from Archaeoglobus… · the same entry in another collection · chain L against L, TM-score 1.00
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 O29976
- Elsewhere: RCSB PDB 2XME · PDBe 2XME · UniProt O29976
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