Research workbench
Human glutathione-S-transferase T1-1, apo form
Analyse Human glutathione-S-transferase T1-1, apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C3N
- Type
- protein
- Length
- 956 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase theta 1
- EC
- 2.5.1.18
- UniProt
- P30711
- Ligands
- IOD
- Pockets
- 8 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Glutathione S-transferase theta 1 (EC 2.5.1.18) | protein | 239 | 64% helix, 7% strand | P30711 |
Ligands and binding sites
- IOD · Iodide ion · ion · 15 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 939 | 0.86 | 0.87 | 91 | IOD |
| 2 | 431 | 0.80 | 0.88 | 49 | IOD |
| 3 | 437 | 0.78 | 0.86 | 42 | IOD |
| 4 | 98 | 0.38 | 0.76 | 17 | empty |
| 5 | 90 | 0.36 | 0.75 | 17 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1472 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1460 Ų buried · 10 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 P30711
- Elsewhere: RCSB PDB 2C3N · PDBe 2C3N · UniProt P30711
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