Research workbench
Crystal structure of NAD(P)H-flavin oxidoreductase (nfor) from S. aureus complexed with reduced FMN and NAD+
Analyse Crystal structure of NAD(P)H-flavin oxidoreductase (nfor) from S. aureus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JH4
- Type
- protein
- Length
- 1,115 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A220YLK3
- Ligands
- FNR, NAD
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | — | protein | 223 | — | A0A220YLK3 |
Ligands and binding sites
- FNR · 1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydro-2H-benzo[g]pteridin-1-id-10(5H)-yl)-5-O-phosphonato-D-ribitol · ligand · 5 copies · chains A, B, C, D, E
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7JH4 · Crystal structure of NAD(P)H-flavin oxidoreductase (NfoR) from S. aureus complexed 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 A0A220YLK3
- Elsewhere: RCSB PDB 7JH4 · PDBe 7JH4 · UniProt A0A220YLK3
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