Research workbench
Structure of drag-glnz-DELTA42-54 complex from azospirillum brasilense
Analyse Structure of drag-glnz-DELTA42-54 complex from azospirillum brasilense in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OVO
- Type
- protein
- Length
- 394 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosyl-(dinitrogen reductase) hydrolase; Nitrogen regulatory protein P-II 1
- UniProt
- A7XNI2, P70731
- Ligands
- ADP, MG, MN
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosyl-(dinitrogen reductase) hydrolase | protein | 295 | 66% helix, 2% strand | A7XNI2 |
| B | Nitrogen regulatory protein P-II 1 | protein | 99 | 29% helix, 33% strand | P70731 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A
- MN · Manganese (II) ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.56 | 0.77 | 31 | ADP, MG |
| 2 | 204 | 0.51 | 0.77 | 43 | MN |
| 3 | 64 | 0.33 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 718 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5OVO · Structure of DraG-GlnZ-delta42-54 complex from Azospirillum brasilense · 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 A7XNI2
- Every structure of UniProt P70731
- Elsewhere: RCSB PDB 5OVO · PDBe 5OVO · UniProt A7XNI2 · UniProt P70731
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