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The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (rmla). ttp complex.
Analyse The structural basis of the catalytic mechanism and regulation of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G2V
- Type
- protein
- Length
- 2,336 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-1-phosphate thymidylyltransferase
- EC
- 2.7.7.24
- UniProt
- Q9HU22
- Ligands
- TTP
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Glucose-1-phosphate thymidylyltransferase (EC 2.7.7.24) | protein | 292 | 38% helix, 23% strand | Q9HU22 |
Ligands and binding sites
- TTP · Thymidine-5'-triphosphate · ligand · 16 copies · chains A, C, B, D, E, G, F, H
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 | 93 | 0.78 | 0.98 | 16 | empty |
| 2 | 82 | 0.77 | 0.99 | 17 | empty |
| 3 | 80 | 0.77 | 0.99 | 16 | empty |
| 4 | 78 | 0.77 | 0.99 | 16 | empty |
| 5 | 382 | 0.75 | 0.85 | 39 | TTP |
Interfaces
15 interfaces between chains.
- F–H · 1962 Ų buried · 45 hydrogen bonds · protein-protein
- B–D · 1956 Ų buried · 40 hydrogen bonds · protein-protein
- E–G · 1940 Ų buried · 38 hydrogen bonds · protein-protein
- A–C · 1938 Ų buried · 38 hydrogen bonds · protein-protein
- E–F · 1306 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1G2V · The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… · the same entry in another collection · chain D against D, 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 Q9HU22
- Elsewhere: RCSB PDB 1G2V · PDBe 1G2V · UniProt Q9HU22
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