Research workbench
X-ray structure of elbb from E. COLI. northeast structural genomics research consortium (nesg) target ER105
Analyse X-ray structure of elbb from E. COLI. northeast structural genomics research… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OY1
- Type
- protein
- Length
- 874 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative sigma cross-reacting protein 27A
- UniProt
- P0ABU5
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative sigma cross-reacting protein 27A | protein | 221 | 38% helix, 17% strand | P0ABU5 |
| B | Putative sigma cross-reacting protein 27A | protein | 219 | 38% helix, 17% strand | P0ABU5 |
| C | Putative sigma cross-reacting protein 27A | protein | 217 | 39% helix, 18% strand | P0ABU5 |
| D | Putative sigma cross-reacting protein 27A | protein | 217 | 38% helix, 18% strand | P0ABU5 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 690 | 0.71 | 0.78 | 59 | empty |
| 2 | 162 | 0.50 | 0.78 | 20 | empty |
| 3 | 166 | 0.50 | 0.78 | 21 | empty |
| 4 | 179 | 0.49 | 0.77 | 20 | empty |
| 5 | 50 | 0.28 | 0.75 | 15 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1589 Ų buried · 30 hydrogen bonds · protein-protein
- A–B · 1588 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 163 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 23 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 28 modified (engineered).
Compared structures
- 1OY1 · X-Ray Structure Of ElbB From E. Coli. Northeast Structural Genomics Research Consortium… · the same entry in another collection · chain D against D, TM-score 1.00
- P0ABU5 · AlphaFold monomer V2.0 prediction for glyoxalase elbb (P0ABU5) · a predicted model of the same protein · chain C 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 P0ABU5
- Elsewhere: RCSB PDB 1OY1 · PDBe 1OY1 · UniProt P0ABU5
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