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KAPOSI'S sarcoma herpesvirus protease in complex with allosteric inhibitor

Analyse KAPOSI'S sarcoma herpesvirus protease in complex with allosteric inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UVP
Type: protein
Length: 380 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Orf 17
UniProt: O40922
Ligands: 8N7
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Orf 17	protein	190	32% helix, 28% strand	O40922
B	Orf 17	protein	190	31% helix, 27% strand	O40922

Ligands and binding sites

8N7 · 6-(cyclohexylmethyl)-N-{2-[(oxan-4-yl)oxy]-4-(1H-tetrazol-5-yl)phenyl}pyridine-2-carboxamide · ligand · 3 copies · chains A, 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	738	0.71	0.77	69	empty
2	177	0.54	0.78	21	8N7
3	86	0.38	0.76	14	8N7

Interfaces

1 interface between chains.

A–B · 760 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5UVP · Kaposi's Sarcoma Herpesvirus Protease in Complex with Allosteric Inhibitor · 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 O40922
Elsewhere: RCSB PDB 5UVP · PDBe 5UVP · UniProt O40922

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