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X-ray crystal structure of the HIV protease complex with L- 700,417, an inhibitor with pseudo C2 symmetry

Analyse X-ray crystal structure of the HIV protease complex with L- 700,417, an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PHV
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease
UniProt: P12497
Ligands: VAC
Pockets: 1 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease	protein	99	7% helix, 56% strand	P12497

Ligands and binding sites

VAC · N,N-bis(2-hydroxy-1-indanyl)-2,6- diphenylmethyl-4-hydroxy-1,7-heptandiamide · 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	351	0.71	0.83	39	VAC

Interfaces

1 interface between chains.

A–B · 1849 Å² buried · 41 hydrogen bonds · protein-protein

Compared structures

4PHV · X-ray crystal structure of the HIV protease complex with L-700,417, an inhibitor with… · 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 P12497
Elsewhere: RCSB PDB 4PHV · PDBe 4PHV · UniProt P12497

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