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Crystal Structure of Unliganded, Full Length hUGDH at pH 7.0
Analyse Crystal Structure of Unliganded, Full Length hUGDH at pH 7.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RJT
- Type
- protein
- Length
- 1,380 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.7
- Source
- Homo sapiens
- Molecule
- UDP-glucose 6-dehydrogenase
- EC
- 1.1.1.22
- UniProt
- O60701
- Ligands
- CL
- Pockets
- 12 · best druggability 0.74
Structure
x-ray diffraction · resolution 2.7 · 3 distinct chains · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UDP-glucose 6-dehydrogenase (EC 1.1.1.22) | protein | 459 | 45% helix, 15% strand | O60701 |
| B | UDP-glucose 6-dehydrogenase (EC 1.1.1.22) | protein | 460 | 44% helix, 15% strand | O60701 |
| C | UDP-glucose 6-dehydrogenase (EC 1.1.1.22) | protein | 461 | 45% helix, 15% strand | O60701 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 787 | 0.74 | 0.79 | 81 | empty |
| 2 | 477 | 0.70 | 0.80 | 48 | empty |
| 3 | 492 | 0.69 | 0.80 | 52 | empty |
| 4 | 183 | 0.62 | 0.83 | 24 | empty |
| 5 | 389 | 0.61 | 0.77 | 52 | empty |
Interfaces
3 interfaces between chains.
- B–C · 719 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 717 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 701 Ų buried · 13 hydrogen bonds · protein-protein
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 O60701
- Elsewhere: RCSB PDB 4RJT · PDBe 4RJT · UniProt O60701
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