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The crystal structure of pii protein
Analyse The crystal structure of pii protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z0G
- Type
- protein
- Length
- 380 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrogen regulatory protein P-II
- UniProt
- O66513
- Ligands
- PO4, CL
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Nitrogen regulatory protein P-II | protein | 95 | 34% helix, 37% strand | O66513 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 10 copies · chains A, B, C, D
- CL · Chloride ion · ion · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.60 | 0.86 | 21 | PO4 |
| 2 | 112 | 0.60 | 0.86 | 21 | PO4 |
| 3 | 114 | 0.59 | 0.85 | 23 | PO4 |
| 4 | 147 | 0.43 | 0.75 | 16 | empty |
Interfaces
5 interfaces between chains.
- A–C · 1181 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1181 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1177 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 243 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 78 Ų buried · 0 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 O66513
- Elsewhere: RCSB PDB 2Z0G · PDBe 2Z0G · UniProt O66513
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