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Structure of urate oxidase from bacillus subtilis 168

Analyse Structure of urate oxidase from bacillus subtilis 168 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6A4M
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uric acid degradation bifunctional protein pucl
EC: 4.1.1.97, 1.7.3.3
UniProt: O32141
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uric acid degradation bifunctional protein pucl (EC 4.1.1.97, 1.7.3.3)	protein	269	25% helix, 42% strand	O32141

Ligands and binding sites

GOL · Glycerol · additive · 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	308	0.68	0.83	50	empty

Compared structures

6A4M · Structure of urate oxidase from Bacillus subtilis 168 · the same entry in another collection · chain A against A, TM-score 1.00
O32141 · AlphaFold monomer V2.0 prediction for uric acid degradation bifunctional protein pucl… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O32141
Elsewhere: RCSB PDB 6A4M · PDBe 6A4M · UniProt O32141

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