MolNFT v1 · #121520 · protein

High resolution structure of barbiturase

5HY1: “High resolution structure of barbiturase”. X-ray diffraction, 3 ligands (WDL, NA, CL), 3 pockets (best druggability 0.48). MolNFT v1 #121520 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5HY1
Type: protein
Length: 367 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Barbiturase
EC: 3.5.2.1
UniProt: Q8RSQ2
Ligands: WDL, NA, CL
Pockets: 3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Barbiturase (EC 3.5.2.1)	protein	367	33% helix, 25% strand	Q8RSQ2

Ligands and binding sites

WDL · 1,3,5-triazine-2,4,6-triol · ligand · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · 3 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	170	0.48	0.76	34	empty
2	123	0.42	0.76	26	empty
3	62	0.28	0.73	17	empty

Compared structures

5HY1 · high resolution structure of barbiturase · the same entry in another collection · chain A against A, TM-score 1.00
Q8RSQ2 · AlphaFold monomer V2.0 prediction for barbiturase (Q8RSQ2) · a predicted model of the same protein · 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 Q8RSQ2
Elsewhere: RCSB PDB 5HY1 · PDBe 5HY1 · UniProt Q8RSQ2

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