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Structure of URT1 in complex with UTP
Analyse Structure of URT1 in complex with UTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L8K
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UTP:RNA uridylyltransferase 1
- EC
- 2.7.7.52
- UniProt
- O64642
- Ligands
- UTP
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UTP:RNA uridylyltransferase 1 (EC 2.7.7.52) | protein | 321 | 45% helix, 17% strand | O64642 |
Ligands and binding sites
- UTP · Uridine 5'-triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 191 | 0.51 | 0.77 | 36 | empty |
| 2 | 249 | 0.49 | 0.74 | 29 | UTP |
| 3 | 77 | 0.35 | 0.76 | 15 | empty |
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 O64642
- Elsewhere: RCSB PDB 6L8K · PDBe 6L8K · UniProt O64642
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