MolNFT v1 · #18695 · protein
A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate
1PX7 · Glutathione S-transferase P: “A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the…”. X-ray diffraction, 2 ligands (GSH, CA), 4 pockets (best druggability 0.71). MolNFT v1 #18695 on…
- PDB
- 1PX7
- Type
- protein
- Length
- 417 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase P
- EC
- 2.5.1.18
- UniProt
- P09211
- Ligands
- GSH, CA
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase P (EC 2.5.1.18) | protein | 209 | 63% helix, 9% strand | P09211 |
| B | Glutathione S-transferase P (EC 2.5.1.18) | protein | 208 | 61% helix, 9% strand | P09211 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · chains B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 650 | 0.71 | 0.79 | 76 | GSH |
| 2 | 100 | 0.38 | 0.76 | 21 | empty |
| 3 | 82 | 0.36 | 0.75 | 17 | empty |
| 4 | 64 | 0.30 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1308 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1PX7 · A folding mutant of human class pi glutathione transferase, created by mutating aspartate… · 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 P09211
- Elsewhere: RCSB PDB 1PX7 · PDBe 1PX7 · UniProt P09211
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