MolNFT v1 · #121463 · protein

High resolution structure of barbiturase

5HWE: “High resolution structure of barbiturase”. X-ray diffraction, 3 ligands (MHA, MG, SO4), 5 pockets (best druggability 0.65). MolNFT v1 #121463 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5HWE
Type: protein
Length: 370 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: MHA, MG, SO4
Pockets: 5 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Barbiturase (EC 3.5.2.1)	protein	370	33% helix, 24% strand	Q8RSQ2

Ligands and binding sites

MHA · (carbamoylmethyl-carboxymethyl-amino)-acetic acid · ligand · chains A
MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

5 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	58	0.65	0.95	20	MHA
2	92	0.50	0.82	18	empty
3	127	0.44	0.77	27	empty
4	91	0.35	0.75	19	empty
5	55	0.32	0.76	17	empty

Compared structures

5HWE · 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 0.99

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 5HWE · PDBe 5HWE · UniProt Q8RSQ2

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