Research workbench
Human glutathione transferase A4-4 with gsdhn
Analyse Human glutathione transferase A4-4 with gsdhn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IK7
- Type
- protein
- Length
- 878 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase A4
- EC
- 2.5.1.18
- UniProt
- O15217
- Ligands
- BOB, SO4
- Pockets
- 11 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase A4 (EC 2.5.1.18) | protein | 221 | 58% helix, 7% strand | O15217 |
| B | Glutathione S-transferase A4 (EC 2.5.1.18) | protein | 219 | 59% helix, 7% strand | O15217 |
| C | Glutathione S-transferase A4 (EC 2.5.1.18) | protein | 218 | 59% helix, 8% strand | O15217 |
| D | Glutathione S-transferase A4 (EC 2.5.1.18) | protein | 220 | 58% helix, 7% strand | O15217 |
Ligands and binding sites
- BOB · (S)-2-amino-5-((R)-1-(carboxymethylamino)-3-((3S,4R)-1,4-dihydroxynonan-3-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 937 | 0.75 | 0.78 | 89 | BOB |
| 2 | 808 | 0.74 | 0.78 | 89 | BOB |
| 3 | 82 | 0.63 | 0.90 | 21 | empty |
| 4 | 81 | 0.62 | 0.90 | 18 | empty |
| 5 | 172 | 0.40 | 0.72 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1449 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 1377 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 712 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
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 O15217
- Elsewhere: RCSB PDB 3IK7 · PDBe 3IK7 · UniProt O15217
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