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I84V HIV-1 protease mutant in complex with a carbamoyl decorated pyrrolidine-based inhibitor

Analyse I84V HIV-1 protease mutant in complex with a carbamoyl decorated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2R38
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
EC: 3.4.23.16
UniProt: Q5RZ08
Ligands: G4G, CL
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease (EC 3.4.23.16)	protein	99	4% helix, 56% strand	Q5RZ08

Ligands and binding sites

G4G · 4,4'-{(3S,4S)-pyrrolidine-3,4-diylbis[(benzylimino)sulfonyl]}dibenzamide · ligand · chains A, B
CL · Chloride ion · ion · 2 copies · chains 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	373	0.75	0.85	34	G4G

Interfaces

1 interface between chains.

A–B · 1844 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

2R38 · I84V HIV-1 protease mutant in complex with a carbamoyl decorated pyrrolidine-based… · 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 Q5RZ08
Elsewhere: RCSB PDB 2R38 · PDBe 2R38 · UniProt Q5RZ08

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