Research workbench
POA1P in complex with ADP-ribose
Analyse POA1P 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
- 6LFR
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribose 1''-phosphate phosphatase
- EC
- 3.1.3.84, 3.2.2.-
- UniProt
- P38218
- Ligands
- APR
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 37% 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 | 37% helix, 22% strand | P38218 |
Ligands and binding sites
- APR · Adenosine-5-diphosphoribose · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.60 | 0.82 | 30 | APR |
| 2 | 51 | 0.29 | 0.75 | 11 | empty |
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 6LFR · PDBe 6LFR · UniProt P38218
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