Research workbench

Xena - reduced - Y183F variant in complex with 8-hydroxycoumarin

Analyse Xena - reduced - Y183F variant in complex with 8-hydroxycoumarin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UTM
Type: protein
Length: 360 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xenobiotic reductase
EC: 1.6.99.1
UniProt: Q3ZDM6
Ligands: FNR, 8CM, SO4
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xenobiotic reductase (EC 1.6.99.1)	protein	360	40% helix, 16% strand	Q3ZDM6

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 · chains A
8CM · 8-hydroxycoumarin · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	547	0.71	0.79	49	FNR, 8CM

Compared structures

4UTM · XenA - Reduced - Y183F variant in complex with 8-hydroxycoumarin · 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 Q3ZDM6
Elsewhere: RCSB PDB 4UTM · PDBe 4UTM · UniProt Q3ZDM6

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