Research workbench
Crystal structure of SARO_2595 from novosphingobium aromaticivorans
Analyse Crystal structure of SARO_2595 from novosphingobium aromaticivorans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UUO
- Type
- protein
- Length
- 569 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase-like protein
- UniProt
- Q2G542
- Ligands
- GSH, SO4
- Pockets
- 6 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Glutathione S-transferase-like protein | protein | 284 | 51% helix, 9% strand | Q2G542 |
| A | Glutathione S-transferase-like protein | protein | 285 | 51% helix, 9% strand | Q2G542 |
Ligands and binding sites
- GSH · Glutathione · ligand · 4 copies · chains B, A
- SO4 · Sulfate ion · ion · 4 copies · chains B, A
- EDO · 1,2-ethanediol · additive · 18 copies · chains B, 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 | 800 | 0.83 | 0.85 | 66 | GSH, EDO |
| 2 | 757 | 0.82 | 0.85 | 68 | GSH, EDO |
| 3 | 54 | 0.32 | 0.77 | 13 | EDO |
| 4 | 63 | 0.32 | 0.76 | 13 | EDO |
| 5 | 57 | 0.30 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- B–A · 3595 Ų buried · 51 hydrogen bonds · protein-protein
Compared structures
- 5UUO · Crystal structure of SARO_2595 from Novosphingobium aromaticivorans · the same entry in another collection · chain B against B, 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 Q2G542
- Elsewhere: RCSB PDB 5UUO · PDBe 5UUO · UniProt Q2G542
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