MolNFT v1 · #11194 · protein
X-ray structure of nitric oxide reductase (cytochrome P450NOR) in the ferrous co state at atomic resolution
1JFC · Nitric-oxide reductase cytochrome P450 55A1: “X-ray structure of nitric oxide reductase (cytochrome P450NOR) in the ferrous co state at atomic resolution”. X-ray diffraction, 2 ligands (HEM, CMO), 4 pockets (best druggability 0.81).…
- PDB
- 1JFC
- Type
- protein
- Length
- 399 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitric-oxide reductase cytochrome P450 55A1
- EC
- 1.7.99.7
- UniProt
- P23295
- Ligands
- HEM, CMO
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitric-oxide reductase cytochrome P450 55A1 (EC 1.7.99.7) | protein | 399 | 53% helix, 10% strand | P23295 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CMO · Carbon monoxide · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1099 | 0.81 | 0.82 | 84 | HEM, CMO |
| 2 | 66 | 0.69 | 0.95 | 22 | empty |
| 3 | 53 | 0.38 | 0.81 | 16 | GOL |
| 4 | 57 | 0.32 | 0.76 | 13 | empty |
Compared structures
- 1JFC · X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferrous CO state at… · 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 1JFC · PDBe 1JFC · UniProt P23295
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