Research workbench
Structure of pii signaling protein glnz from azospirillum brasilense in complex with adenosine triphosphate
Analyse Structure of pii signaling protein glnz from azospirillum brasilense in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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