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Crystal structure of a flavoenzyme ruta in the pyrimidine catabolic pathway

Analyse Crystal structure of a flavoenzyme ruta in the pyrimidine catabolic pathway in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WAN
Type: protein
Length: 341 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyrimidine monooxygenase ruta
EC: 1.14.99.46
UniProt: A0A1R1KFF4
Ligands: URA, FMN, SO4
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyrimidine monooxygenase ruta (EC 1.14.99.46)	protein	341	41% helix, 19% strand	A0A1R1KFF4

Ligands and binding sites

URA · Uracil · ligand · chains A
FMN · Flavin mononucleotide · ligand · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A
GOL · Glycerol · additive · 3 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	476	0.73	0.82	43	URA, FMN

Compared structures

5WAN · Crystal Structure of a flavoenzyme RutA in the pyrimidine catabolic pathway · 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 A0A1R1KFF4
Elsewhere: RCSB PDB 5WAN · PDBe 5WAN · UniProt A0A1R1KFF4

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