MolNFT v2 · #30075 · protein
The structure of gene product APE0525 from Aeropyrum pernix
1ZS7 · hypothetical protein APE0525: “The structure of gene product APE0525 from Aeropyrum pernix”. X-ray diffraction at 1.85, 2 ligands (K, PO4), 2 pockets (best druggability 0.38). MolNFT v2 #30075 on GenesisL1: 3D structure, binding…
- PDB
- 1ZS7
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Aeropyrum pernix
- Molecule
- hypothetical protein APE0525
- UniProt
- Q9YEQ6
- Ligands
- K, PO4
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · resolution 1.85 · 1 distinct chain · 29% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | hypothetical protein APE0525 | protein | 187 | 29% helix, 37% strand | Q9YEQ6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.38 | 0.78 | 15 | empty |
| 2 | 54 | 0.28 | 0.74 | 12 | empty |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 1ZS7 · The structure of gene product APE0525 from aeropyrum pernix · 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 Q9YEQ6
- Elsewhere: RCSB PDB 1ZS7 · PDBe 1ZS7 · UniProt Q9YEQ6
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