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Crystal structure of Poa1p in apo form
Analyse Crystal structure of Poa1p in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LFQ
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.359
- Source
- Saccharomyces cerevisiae S288c
- Molecule
- ADP-ribose 1''-phosphate phosphatase
- EC
- 3.1.3.84, 3.2.2.-
- UniProt
- P38218
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · resolution 2.359 · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribose 1''-phosphate phosphatase (EC 3.1.3.84, 3.2.2.-) | protein | 169 | 38% helix, 21% strand | P38218 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.60 | 0.81 | 30 | GOL |
Compared structures
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 P38218
- Elsewhere: RCSB PDB 6LFQ · PDBe 6LFQ · UniProt P38218
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