Research workbench
Crystal structure of CTP:GLYCEROL-3-phosphate cytidylyltransferase from staphylococcus aureus
Analyse Crystal structure of CTP:GLYCEROL-3-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
- 2B7L
- Type
- protein
- Length
- 454 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycerol-3-phosphate cytidylyltransferase
- EC
- 2.7.7.39
- UniProt
- O05155
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate cytidylyltransferase (EC 2.7.7.39) | protein | 115 | 37% helix, 23% strand | O05155 |
| B, C, D | Glycerol-3-phosphate cytidylyltransferase (EC 2.7.7.39) | protein | 113 | 38% helix, 24% strand | O05155 |
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 | 1009 | 0.80 | 0.81 | 86 | empty |
| 2 | 136 | 0.46 | 0.77 | 28 | empty |
| 3 | 153 | 0.46 | 0.76 | 25 | empty |
Interfaces
6 interfaces between chains.
- A–B · 749 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 743 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 294 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 280 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 249 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2B7L · Crystal Structure of CTP:Glycerol-3-Phosphate Cytidylyltransferase from Staphylococcus… · the same entry in another collection · chain A against A, 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 O05155
- Elsewhere: RCSB PDB 2B7L · PDBe 2B7L · UniProt O05155
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