Research workbench
PCE1 guanylyltransferase
Analyse PCE1 guanylyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PZ7
- Type
- protein
- Length
- 746 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MRNA-capping enzyme subunit alpha
- EC
- 2.7.7.50
- UniProt
- P40997
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | MRNA-capping enzyme subunit alpha (EC 2.7.7.50) | protein | 373 | 28% helix, 33% strand | P40997 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 918 | 0.80 | 0.82 | 100 | SO4, GOL |
| 2 | 265 | 0.53 | 0.76 | 33 | empty |
| 3 | 171 | 0.51 | 0.78 | 19 | empty |
| 4 | 103 | 0.46 | 0.79 | 18 | GOL |
| 5 | 84 | 0.44 | 0.80 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1068 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
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 P40997
- Elsewhere: RCSB PDB 4PZ7 · PDBe 4PZ7 · UniProt P40997
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