Research workbench
Crystal structure of ZMPSTE24
Analyse Crystal structure of ZMPSTE24 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SYT
- Type
- protein
- Length
- 444 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caax prenyl protease 1 homolog
- EC
- 3.4.24.84
- UniProt
- O75844
- Ligands
- PC1, CXE, ZN, SO4
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caax prenyl protease 1 homolog (EC 3.4.24.84) | protein | 444 | 71% helix, 3% strand | O75844 |
Ligands and binding sites
- PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · chains A
- CXE · Pentaethylene glycol monodecyl ether · ligand · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 12 copies · chains A
- DMS · Dimethyl sulfoxide · additive · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 992 | 0.75 | 0.77 | 108 | CXE, C8E, DMS |
| 2 | 142 | 0.42 | 0.75 | 17 | empty |
| 3 | 81 | 0.31 | 0.73 | 18 | empty |
Compared structures
- O75844 · AlphaFold monomer V2.0 prediction for caax prenyl protease 1 homolog (O75844) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O75844
- Elsewhere: RCSB PDB 5SYT · PDBe 5SYT · UniProt O75844
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