MolNFT v1 · #26637 · protein
Alpha-D-glucose-1-phosphate cytidylyltransferase complexed with CTP
1WVC: “Alpha-D-glucose-1-phosphate cytidylyltransferase complexed with CTP”. X-ray diffraction, 3 ligands (CTP, MG, NI), 2 pockets (best druggability 0.55). MolNFT v1 #26637 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1WVC
- Type
- protein
- Length
- 254 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-1-phosphate cytidylyltransferase
- EC
- 2.7.7.33
- UniProt
- P26396
- Ligands
- CTP, MG, NI
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-1-phosphate cytidylyltransferase (EC 2.7.7.33) | protein | 254 | 33% helix, 26% strand | P26396 |
Ligands and binding sites
- CTP · Cytidine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- NI · Nickel (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 238 | 0.55 | 0.78 | 29 | MG, CTP |
| 2 | 65 | 0.31 | 0.75 | 14 | empty |
Compared structures
- 1WVC · alpha-D-glucose-1-phosphate cytidylyltransferase complexed with CTP · the same entry in another collection · chain A against A, TM-score 1.00
- P26396 · AlphaFold monomer V2.0 prediction for glucose-1-phosphate cytidylyltransferase (P26396) · 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 P26396
- Elsewhere: RCSB PDB 1WVC · PDBe 1WVC · UniProt P26396
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