Research workbench
Poa1p H23A mutant in complex with ADP-ribose
Analyse Poa1p H23A mutant in complex with ADP-ribose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LFS
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.87
- Source
- Saccharomyces cerevisiae S288c
- Molecule
- ADP-ribose 1''-phosphate phosphatase
- EC
- 3.1.3.84, 3.2.2.-
- UniProt
- P38218
- Ligands
- APR
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · resolution 1.87 · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribose 1''-phosphate phosphatase (EC 3.1.3.84, 3.2.2.-) | protein | 166 | 39% helix, 22% strand | P38218 |
Ligands and binding sites
- APR · Adenosine-5-diphosphoribose · ligand · chains A
- CXS · 3-cyclohexyl-1-propylsulfonic acid · 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 | 180 | 0.60 | 0.82 | 29 | APR, CXS |
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 6LFS · PDBe 6LFS · UniProt P38218
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