Research workbench
Structure of cytochrome P450NOR in no-bound state: damaged by low-dose (0.72 mgy) X-ray
Analyse Structure of cytochrome P450NOR in no-bound state: damaged by low-dose (0.72… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y5F
- Type
- protein
- Length
- 400 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P23295
- Ligands
- HEM, NO
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 400 | — | P23295 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- NO · Nitric oxide · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5Y5F · Structure of cytochrome P450nor in NO-bound state: damaged by low-dose (0.72 MGy) X-ray · the same entry in another collection · chain A against A, TM-score 1.00
- P23295 · AlphaFold monomer V2.0 prediction for NADP nitrous oxide-forming nitric oxide reductase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P23295
- Elsewhere: RCSB PDB 5Y5F · PDBe 5Y5F · UniProt P23295
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