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Crystal structure of HIV-1 protease complexed with pl-100

Analyse Crystal structure of HIV-1 protease complexed with pl-100 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QMP
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein
EC: 3.4.23.16
UniProt: Q9WFL7
Ligands: A00
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pol polyprotein (EC 3.4.23.16)	protein	99	7% helix, 56% strand	Q9WFL7

Ligands and binding sites

A00 · N-[(5S)-5-{[(4-aminophenyl)sulfonyl](isobutyl)amino}-6-hydroxyhexyl]-Nalpha-(methoxycarbonyl)-beta-phenyl-L-phenylalaninamide · ligand · 2 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	392	0.73	0.83	37	A00

Interfaces

1 interface between chains.

A–B · 1848 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

2QMP · Crystal Structure of HIV-1 protease complexed with PL-100 · 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 Q9WFL7
Elsewhere: RCSB PDB 2QMP · PDBe 2QMP · UniProt Q9WFL7

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