MolNFT v1 · #30065 · 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, 2 ligands (K, PO4), 2 pockets (best druggability 0.38). MolNFT v1 #30065 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1ZS7
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein APE0525
- UniProt
- Q9YEQ6
- Ligands
- K, PO4
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 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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