Research workbench
Crystal structure of yeeu from E. COLI. northeast structural genomics target ER304
Analyse Crystal structure of yeeu from E. COLI. northeast structural genomics target… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H28
- Type
- protein
- Length
- 213 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein yeeu
- UniProt
- P76364
- Ligands
- MG, CL
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein yeeu | protein | 109 | 25% helix, 33% strand | P76364 |
| B | Hypothetical protein yeeu | protein | 104 | 26% helix, 35% strand | P76364 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.53 | 0.80 | 30 | GOL |
| 2 | 140 | 0.46 | 0.77 | 21 | MG |
Interfaces
1 interface between chains.
- A–B · 554 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 2H28 · Crystal structure of YeeU from E. coli. Northeast Structural Genomics target ER304 · the same entry in another collection · chain A against A, TM-score 1.00
- P76364 · AlphaFold monomer V2.0 prediction for cytoskeleton bundling-enhancing antitoxin cbea… · a predicted model of the same protein · chain B against A, TM-score 0.96
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 P76364
- Elsewhere: RCSB PDB 2H28 · PDBe 2H28 · UniProt P76364
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