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Resting state copper nitrite reductase determined by serial femtosecond rotation crystallography
Analyse Resting state copper nitrite reductase determined by serial femtosecond… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ONX
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Alcaligenes xylosoxydans xylosoxydans
- Molecule
- Copper-containing nitrite reductase
- EC
- 1.7.2.1
- UniProt
- O68601
- Ligands
- CU, ZN, OXY
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · resolution 1.6 · 1 distinct chain · 10% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper-containing nitrite reductase (EC 1.7.2.1) | protein | 335 | 10% helix, 39% strand | O68601 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
- OXY · Oxygen molecule · ion · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.40 | 0.77 | 16 | empty |
Compared structures
- 5ONX · Resting state copper nitrite reductase determined by serial femtosecond rotation… · 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 O68601
- Elsewhere: RCSB PDB 5ONX · PDBe 5ONX · UniProt O68601
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