Research workbench
Glutathione transferase A3-3 in complex with glutathione and delta-4- androstene-3-17-dione
Analyse Glutathione transferase A3-3 in complex with glutathione and delta-4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VCV
- Type
- protein
- Length
- 3,504 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase A3
- EC
- 2.5.1.18
- UniProt
- Q16772
- Ligands
- GSH, ASD
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | Glutathione S-transferase A3 (EC 2.5.1.18) | protein | 219 | 59% helix, 8% strand | Q16772 |
Ligands and binding sites
- GSH · Glutathione · ligand · 16 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
- ASD · 4-androstene-3-17-dione · ligand · 11 copies · chains A, B, D, E, F, G, H, I, K, L, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1037 | 0.86 | 0.87 | 122 | GSH, ASD |
| 2 | 967 | 0.86 | 0.87 | 112 | GSH |
| 3 | 705 | 0.84 | 0.88 | 91 | GSH, ASD |
| 4 | 1113 | 0.84 | 0.85 | 117 | GSH, ASD |
| 5 | 688 | 0.84 | 0.88 | 87 | GSH, ASD |
Interfaces
26 interfaces between chains.
- O–P · 1592 Ų buried · 20 hydrogen bonds · protein-protein
- I–J · 1581 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1572 Ų buried · 16 hydrogen bonds · protein-protein
- K–L · 1569 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1568 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2VCV · Glutathione transferase A3-3 in complex with glutathione and delta-4… · the same entry in another collection · chain P against P, 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 Q16772
- Elsewhere: RCSB PDB 2VCV · PDBe 2VCV · UniProt Q16772
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