MolNFT v2 · #129971 · protein
Resting state copper nitrite reductase determined by serial femtosecond rotation crystallography
5ONX: “Resting state copper nitrite reductase determined by serial femtosecond rotation crystallography”. X-ray diffraction at 1.6, 3 ligands (CU, ZN, OXY). MolNFT v2 #129971 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- O68601
- Ligands
- CU, ZN, OXY
Structure
x-ray diffraction · resolution 1.6 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 335 | — | 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.
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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