Research workbench

EBV dutpase mutant ASP131ASN with bound dump

Analyse EBV dutpase mutant ASP131ASN with bound dump in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WE1
Type: protein
Length: 245 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, SO4
Pockets: 3 · best druggability 0.50

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	245	4% helix, 50% strand	P03195

Ligands and binding sites

UMP · 2'-deoxyuridine 5'-monophosphate · ligand · chains A
SO4 · Sulfate 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	115	0.50	0.81	18	UMP
2	135	0.42	0.75	24	empty
3	53	0.26	0.74	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2WE1 · EBV dUTPase mutant Asp131Asn with bound dUMP · 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 2WE1 · PDBe 2WE1 · UniProt P03195

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