Research workbench
Crystal structure of universal stress protein E from proteus mirabilis in complex with udp-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha- glucosamine
Analyse Crystal structure of universal stress protein E from proteus mirabilis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WY2
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Universal stress protein E
- UniProt
- B4ETT2
- Ligands
- U20, CL, SO4
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Universal stress protein E | protein | 308 | 43% helix, 21% strand | B4ETT2 |
Ligands and binding sites
- U20 · uridine-5'-diphosphate-3-O-(R-3-hydroxymyristoyl)-N-acetyl-D-glucosamine · ligand · chains A
- CL · Chloride ion · ion · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.66 | 0.87 | 34 | GOL |
| 2 | 123 | 0.63 | 0.87 | 22 | empty |
| 3 | 131 | 0.47 | 0.78 | 22 | empty |
| 4 | 50 | 0.31 | 0.77 | 15 | empty |
| 5 | 53 | 0.30 | 0.76 | 15 | empty |
Compared structures
- 4WY2 · Crystal structure of universal stress protein E from Proteus mirabilis in complex with… · 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 B4ETT2
- Elsewhere: RCSB PDB 4WY2 · PDBe 4WY2 · UniProt B4ETT2
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