Research workbench
Acid anhydride hydrolase
Analyse Acid anhydride hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YPP
- Type
- protein
- Length
- 564 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inorganic pyrophosphatase
- EC
- 3.6.1.1
- UniProt
- P00817
- Ligands
- MN, PO4
- Pockets
- 7 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Inorganic pyrophosphatase (EC 3.6.1.1) | protein | 282 | 17% helix, 31% strand | P00817 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 8 copies · chains A, B
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 661 | 0.65 | 0.75 | 59 | empty |
| 2 | 163 | 0.51 | 0.79 | 30 | MN, PO4 |
| 3 | 130 | 0.50 | 0.80 | 24 | MN, PO4 |
| 4 | 68 | 0.49 | 0.84 | 19 | empty |
| 5 | 61 | 0.47 | 0.84 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 976 Ų buried · 6 hydrogen bonds · protein-protein
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 P00817
- Elsewhere: RCSB PDB 1YPP · PDBe 1YPP · UniProt P00817
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