Research workbench
Crystal structure of a glutathione transferase family member from burkholderia graminis, target efi-507264, no gsh, disordered domains, space group P21, FORM(2)
Analyse Crystal structure of a glutathione transferase family member from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KE3
- Type
- protein
- Length
- 784 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase domain
- UniProt
- B1FZ96
- Pockets
- 10 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase domain | protein | 207 | 53% helix, 9% strand | B1FZ96 |
| C, D | Glutathione S-transferase domain | protein | 185 | 57% helix, 8% strand | B1FZ96 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 557 | 0.65 | 0.76 | 52 | empty |
| 2 | 484 | 0.62 | 0.76 | 53 | empty |
| 3 | 92 | 0.49 | 0.82 | 25 | empty |
| 4 | 78 | 0.48 | 0.83 | 26 | empty |
| 5 | 199 | 0.47 | 0.75 | 23 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1461 Ų buried · 29 hydrogen bonds · protein-protein
- A–D · 1460 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 44 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 41 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4KE3 · Crystal structure of a glutathione transferase family member from Burkholderia graminis… · 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 B1FZ96
- Elsewhere: RCSB PDB 4KE3 · PDBe 4KE3 · UniProt B1FZ96
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