Research workbench

Joint NEUTRON/X-ray structure of urate oxidase in complex with 8- hydroxyxanthine

Analyse Joint NEUTRON/X-ray structure of urate oxidase in complex with 8… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4N9M
Type: protein
Length: 295 residues
Chains: 1
Method: neutron diffraction; x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uricase
EC: 1.7.3.3
UniProt: Q00511
Ligands: ACE, 8HX, NA, CL
Pockets: 2 · best druggability 0.54

Structure

neutron diffraction; x-ray diffraction · 1 distinct chain · 27% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uricase (EC 1.7.3.3)	protein	295	27% helix, 38% strand	Q00511

Ligands and binding sites

ACE · Acetyl group · ligand · chains A
8HX · 8-hydroxy-3,9-dihydro-1H-purine-2,6-dione · ligand · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	206	0.54	0.78	21	empty
2	174	0.46	0.75	23	8HX, CL

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

4N9M · Joint neutron/x-ray structure of urate oxidase in complex with 8-hydroxyxanthine · 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 Q00511
Elsewhere: RCSB PDB 4N9M · PDBe 4N9M · UniProt Q00511

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.