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E. COLI nfsa

Analyse E. COLI nfsa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7Q0O
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxygen-insensitive NADPH nitroreductase
EC: 1.-.-.-
UniProt: P17117
Ligands: FMN

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxygen-insensitive NADPH nitroreductase (EC 1.-.-.-)	protein	240	48% helix, 13% strand	P17117

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7Q0O · E. coli NfsA · the same entry in another collection · chain A against A, TM-score 1.00
P17117 · AlphaFold monomer V2.0 prediction for oxygen-insensitive NADPH nitroreductase (P17117) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P17117
Elsewhere: RCSB PDB 7Q0O · PDBe 7Q0O · UniProt P17117

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