MolNFT v1 · #26457 · protein

Hydrolytic enzyme human cytomegalovirus protease

1WPO: “Hydrolytic enzyme human cytomegalovirus protease”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.42). MolNFT v1 #26457 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1WPO
Type: protein
Length: 419 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human cytomegalovirus protease
EC: 3.4.21.-
UniProt: P16753
Ligands: SO4
Pockets: 3 · best druggability 0.42

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Human cytomegalovirus protease (EC 3.4.21.-)	protein	207	35% helix, 22% strand	P16753
B	Human cytomegalovirus protease (EC 3.4.21.-)	protein	212	36% helix, 24% strand	P16753

Ligands and binding sites

SO4 · Sulfate ion · ion · chains B

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

Pockets

3 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	129	0.42	0.76	27	empty
2	111	0.36	0.74	18	empty
3	52	0.27	0.74	10	empty

Interfaces

1 interface between chains.

A–B · 1547 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

1WPO · Hydrolytic enzyme human cytomegalovirus protease · 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 P16753
Elsewhere: RCSB PDB 1WPO · PDBe 1WPO · UniProt P16753

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