Research workbench
Crystal structure of KEAP1 complexed with prothymosin alpha
Analyse Crystal structure of KEAP1 complexed with prothymosin alpha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z32
- Type
- protein
- Length
- 299 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1; Prothymosin alpha
- UniProt
- Q9Z2X8, P26350
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like ech-associated protein 1 | protein | 290 | 1% helix, 51% strand | Q9Z2X8 |
| B | Prothymosin alpha | protein | 9 | 0% helix, 0% strand | P26350 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 469 | 0.72 | 0.82 | 41 | SO4 |
| 2 | 60 | 0.28 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 519 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 2Z32 · Crystal structure of Keap1 complexed with Prothymosin alpha · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Z2X8 · AlphaFold monomer V2.0 prediction for kelch-like ech-associated protein 1 (Q9Z2X8) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P26350 · AlphaFold monomer V2.0 prediction for prothymosin alpha (P26350) · a predicted model of the same protein · chain B against A, TM-score 0.26
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 Q9Z2X8
- Every structure of UniProt P26350
- Elsewhere: RCSB PDB 2Z32 · PDBe 2Z32 · UniProt Q9Z2X8 · UniProt P26350
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