MolNFT v1 · #112625 · protein
A revised partiality model and post-refinement algorithm for X-ray free-electron laser data
4ZQX · Polyhedrin: “A revised partiality model and post-refinement algorithm for X-ray free-electron laser data”. X-ray diffraction, 2 ligands (ATP, MG), 2 pockets (best druggability 0.34). MolNFT v1 #112625 on GenesisL1: 3D structure…
- PDB
- 4ZQX
- Type
- protein
- Length
- 236 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyhedrin
- UniProt
- Q5EK29
- Ligands
- ATP, MG
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyhedrin | protein | 236 | 29% helix, 28% strand | Q5EK29 |
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 | 64 | 0.34 | 0.77 | 14 | empty |
| 2 | 72 | 0.32 | 0.74 | 21 | empty |
Compared structures
- 4ZQX · A revised partiality model and post-refinement algorithm for X-ray free-electron laser… · 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 Q5EK29
- Elsewhere: RCSB PDB 4ZQX · PDBe 4ZQX · UniProt Q5EK29
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