Research workbench

HCMV DNA polymerase subunit UL44 complex with a small molecule

Analyse HCMV DNA polymerase subunit UL44 complex with a small molecule in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IWD
Type: protein
Length: 261 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.56
Source: Human cytomegalovirus (strain AD169)
Molecule: DNA polymerase processivity factor
UniProt: P16790
Ligands: 6EV
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · resolution 2.56 · 1 distinct chain · 17% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA polymerase processivity factor	protein	261	17% helix, 43% strand	P16790

Ligands and binding sites

6EV · 5-methylidene-3-(methylsulfanyl)-2-benzothiophen-4(5H)-one · ligand · 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	141	0.55	0.82	23	empty
2	93	0.39	0.76	18	6EV
3	81	0.35	0.75	16	empty

Modifications

Observed in the structure: 3 covalent (covalent ligand).

Compared structures

5IWD · Hcmv DNA polymerase subunit UL44 complex with a small molecule · 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 P16790
Elsewhere: RCSB PDB 5IWD · PDBe 5IWD · UniProt P16790

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