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Crystal Structure of Sphingomonas elodea ATCC 31461 Glucose-1- phosphate uridylyltransferase in Complex with glucose-1-phosphate.
Analyse Crystal Structure of Sphingomonas elodea ATCC 31461 Glucose-1- phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UX8
- Type
- protein
- Length
- 2,192 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.65
- Source
- SPHINGOMONAS ELODEA
- Molecule
- Glucose-1-phosphate uridylyltransferase
- EC
- 2.7.7.9
- UniProt
- Q5FYV5
- Ligands
- G1P
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · resolution 2.65 · 8 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) | protein | 255 | 37% helix, 21% strand | Q5FYV5 |
| B | Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) | protein | 280 | 35% helix, 25% strand | Q5FYV5 |
| C | Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) | protein | 282 | 36% helix, 24% strand | Q5FYV5 |
| D | Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) | protein | 281 | 35% helix, 25% strand | Q5FYV5 |
| E | Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) | protein | 280 | 36% helix, 26% strand | Q5FYV5 |
| F | Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) | protein | 282 | 36% helix, 25% strand | Q5FYV5 |
| G | Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) | protein | 288 | 35% helix, 25% strand | Q5FYV5 |
| H | Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) | protein | 244 | 39% helix, 20% strand | Q5FYV5 |
Ligands and binding sites
- G1P · 1-O-phosphono-alpha-D-glucopyranose · sugar · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1015 | 0.89 | 0.91 | 119 | empty |
| 2 | 974 | 0.89 | 0.90 | 119 | empty |
| 3 | 578 | 0.71 | 0.80 | 46 | G1P |
| 4 | 446 | 0.71 | 0.82 | 40 | G1P |
| 5 | 533 | 0.70 | 0.79 | 46 | G1P |
Interfaces
12 interfaces between chains.
- E–H · 2514 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 2509 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 2487 Ų buried · 20 hydrogen bonds · protein-protein
- F–G · 2461 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 1405 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
- 2UX8 · Crystal structure of sphingomonas elodea atcc 31461 glucose-1- phosphate… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5FYV5
- Elsewhere: RCSB PDB 2UX8 · PDBe 2UX8 · UniProt Q5FYV5
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