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Epstein Barr Virus dUTPase in complex with a,b-imino dUTP

Analyse Epstein Barr Virus dUTPase in complex with a,b-imino dUTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BT1
Type: protein
Length: 254 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.7
Source: HUMAN HERPESVIRUS 4
Molecule: Deoxyuridine 5'-triphosphate nucleotidohydrolase
EC: 3.6.1.23
UniProt: P03195
Ligands: DUP, MG
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · resolution 2.7 · 1 distinct chain · 4% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC 3.6.1.23)	protein	254	4% helix, 48% strand	P03195

Ligands and binding sites

DUP · 2'-deoxyuridine 5'-alpha,beta-imido-triphosphate · ligand · chains A
MG · Magnesium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	165	0.48	0.77	25	DUP, MG
2	107	0.40	0.76	24	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2BT1 · Epstein barr virus dutpase in complex with A,B-imino dutp · 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 2BT1 · PDBe 2BT1 · UniProt P03195

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