Research workbench
Pyruvate phosphate dikinase
Analyse Pyruvate phosphate dikinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DIK
- Type
- protein
- Length
- 869 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyruvate phosphate dikinase
- EC
- 2.7.9.1
- UniProt
- P22983
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyruvate phosphate dikinase (EC 2.7.9.1) | protein | 869 | 47% helix, 17% strand | P22983 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
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 | 727 | 0.80 | 0.84 | 73 | SO4 |
| 2 | 922 | 0.73 | 0.77 | 74 | empty |
| 3 | 233 | 0.57 | 0.78 | 37 | empty |
| 4 | 206 | 0.48 | 0.75 | 39 | SO4 |
| 5 | 98 | 0.39 | 0.76 | 21 | 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 P22983
- Elsewhere: RCSB PDB 1DIK · PDBe 1DIK · UniProt P22983
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