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HIV-1 Protease in complex with amidhyroxysulfone

Analyse HIV-1 Protease in complex with amidhyroxysulfone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XL5
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.73
Source: Human immunodeficiency virus 1
Molecule: Protease retropepsin
EC: 3.4.23.16
UniProt: P03367
Ligands: 190, CL
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · resolution 1.73 · 1 distinct chain · 4% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease retropepsin (EC 3.4.23.16)	protein	99	4% helix, 55% strand	P03367

Ligands and binding sites

190 · N-{(1S)-1-(3-bromobenzyl)-4-[(4-bromophenyl)sulfonyl]-6-methyl-2-oxoheptyl}-2-(2,6-dimethylphenoxy)acetamide · ligand · chains A, B
CL · Chloride ion · ion · 3 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	382	0.71	0.83	39	190

Interfaces

1 interface between chains.

A–B · 1840 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

1XL5 · HIV-1 protease in complex with amidhyroxysulfone · 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 P03367
Elsewhere: RCSB PDB 1XL5 · PDBe 1XL5 · UniProt P03367

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