Research workbench

EBV dutpase mutant CYS4SER

Analyse EBV dutpase mutant CYS4SER in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WE0
Type: protein
Length: 247 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deoxyuridine 5'-triphosphate nucleotidohydrolase
EC: 3.6.1.23
UniProt: P03195
Ligands: UMP, TEO, SO4
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC 3.6.1.23)	protein	247	4% helix, 50% strand	P03195

Ligands and binding sites

UMP · 2'-deoxyuridine 5'-monophosphate · ligand · chains A
TEO · Malate like intermediate · ligand · chains A
SO4 · Sulfate 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	159	0.51	0.79	22	UMP, TEO
2	159	0.44	0.75	33	empty

Compared structures

2WE0 · EBV dUTPase mutant Cys4Ser · 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 P03195
Elsewhere: RCSB PDB 2WE0 · PDBe 2WE0 · UniProt P03195

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