MolNFT v1 · #88218 · protein
Structure of pii signaling protein glnz from azospirillum brasilense in complex with adenosine triphosphate
4CO4 · Pii-like protein pz: “Structure of pii signaling protein glnz from azospirillum brasilense in complex with adenosine triphosphate”. X-ray diffraction, 3 ligands (ATP, AMP, PO4), 3 pockets (best druggability 0.57). MolNFT v1 #88218…
- PDB
- 4CO4
- Type
- protein
- Length
- 272 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pii-like protein pz
- UniProt
- P70731
- Ligands
- ATP, AMP, PO4
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Pii-like protein pz | protein | 90 | 28% helix, 40% strand | P70731 |
| B | Pii-like protein pz | protein | 92 | 27% helix, 40% strand | P70731 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, C, B
- AMP · Adenosine monophosphate · ligand · chains B, C
- PO4 · Phosphate ion · ion · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.57 | 0.79 | 37 | ATP |
| 2 | 230 | 0.57 | 0.78 | 36 | PO4, AMP |
| 3 | 177 | 0.55 | 0.80 | 31 | ATP |
Interfaces
3 interfaces between chains.
- A–C · 1003 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 990 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 931 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4CO4 · Structure of PII signaling protein GlnZ from Azospirillum brasilense in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
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 P70731
- Elsewhere: RCSB PDB 4CO4 · PDBe 4CO4 · UniProt P70731
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