Research workbench
E. COLI bifunctional glutathionylspermidine SYNTHETASE/AMIDASE apo protein
Analyse E. COLI bifunctional glutathionylspermidine SYNTHETASE/AMIDASE apo protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IOB
- Type
- protein
- Length
- 1,153 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional glutathionylspermidine SYNTHETASE/AMIDASE
- EC
- 6.3.1.8, 3.5.1.78
- UniProt
- P0AES0
- Pockets
- 11 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional glutathionylspermidine SYNTHETASE/AMIDASE (EC 6.3.1.8, 3.5.1.78) | protein | 571 | 28% helix, 28% strand | P0AES0 |
| B | Bifunctional glutathionylspermidine SYNTHETASE/AMIDASE (EC 6.3.1.8, 3.5.1.78) | protein | 582 | 28% helix, 29% strand | P0AES0 |
Pockets
11 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1039 | 0.85 | 0.86 | 141 | empty |
| 2 | 737 | 0.73 | 0.79 | 73 | empty |
| 3 | 705 | 0.70 | 0.77 | 68 | empty |
| 4 | 184 | 0.70 | 0.88 | 30 | empty |
| 5 | 224 | 0.69 | 0.86 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 1826 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2IOB · E. coli Bifunctional glutathionylspermidine synthetase/amidase Apo protein · the same entry in another collection · chain A against A, TM-score 1.00
- P0AES0 · AlphaFold monomer V2.0 prediction for bifunctional glutathionylspermidine… · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P0AES0
- Elsewhere: RCSB PDB 2IOB · PDBe 2IOB · UniProt P0AES0
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