Research workbench
Crystal structure of gumk in complex with udp
Analyse Crystal structure of gumk in complex with udp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q6V
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucuronosyltransferase gumk
- EC
- 2.4.1.17
- UniProt
- Q8GCH2
- Ligands
- UDP
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucuronosyltransferase gumk (EC 2.4.1.17) | protein | 370 | 39% helix, 19% strand | Q8GCH2 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · 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 | 819 | 0.77 | 0.80 | 66 | UDP |
| 2 | 141 | 0.49 | 0.79 | 29 | empty |
| 3 | 54 | 0.44 | 0.84 | 19 | 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 Q8GCH2
- Elsewhere: RCSB PDB 2Q6V · PDBe 2Q6V · UniProt Q8GCH2
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