Research workbench
Structure of pii signaling protein glnz from azospirillum brasilense in complex with adenosine diphosphate
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
- 4CO0
- Type
- protein
- Length
- 216 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pii-like protein pz
- UniProt
- P70731
- Ligands
- ADP
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pii-like protein pz | protein | 109 | 27% helix, 37% strand | P70731 |
| B | Pii-like protein pz | protein | 107 | 27% helix, 34% strand | P70731 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- TLA · L(+)-tartaric acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 64 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4CO0 · 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 4CO0 · PDBe 4CO0 · UniProt P70731
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.