Research workbench
POA1P F152A mutant in complex with ADP-ribose
Analyse POA1P F152A 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
- 6LFU
- Type
- protein
- Length
- 325 residues
- Chains
- 2
- 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
- 3 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 36% 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 | 165 | 37% helix, 21% strand | P38218 |
| B | ADP-ribose 1''-phosphate phosphatase (EC 3.1.3.84, 3.2.2.-) | protein | 160 | 35% helix, 21% strand | P38218 |
Ligands and binding sites
- APR · Adenosine-5-diphosphoribose · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 918 | 0.81 | 0.82 | 88 | APR |
| 2 | 54 | 0.35 | 0.78 | 17 | empty |
| 3 | 55 | 0.26 | 0.73 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 165 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 6LFU · PDBe 6LFU · UniProt P38218
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