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Structure of F306C mutant of nitrite reductase from achromobacter xylosoxidans with nitrite bound
Analyse Structure of F306C mutant of nitrite reductase from achromobacter xylosoxidans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CSZ
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dissimilatory copper-containing nitrite reductase
- EC
- 1.7.2.1
- UniProt
- O68601
- Ligands
- ZN, CU, NO2
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dissimilatory copper-containing nitrite reductase (EC 1.7.2.1) | protein | 335 | 11% helix, 39% strand | O68601 |
Ligands and binding sites
- ZN · Zinc ion · metal · 7 copies · chains A
- CU · Copper (II) ion · metal · 2 copies · chains A
- NO2 · Nitrite ion · ion · chains A
- PEG · Di(hydroxyethyl)ether · 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 | 84 | 0.42 | 0.79 | 17 | ZN |
Compared structures
- 4CSZ · STRUCTURE OF F306C MUTANT OF NITRITE REDUCTASE FROM Achromobacter XYLOSOXIDANS 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 O68601
- Elsewhere: RCSB PDB 4CSZ · PDBe 4CSZ · UniProt O68601
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