MolNFT v1 · #78480 · protein

Crystal structure of wild-type HIV-1 protease in complex with AF77

3SAA: “Crystal structure of wild-type HIV-1 protease in complex with AF77”. X-ray diffraction, 2 ligands (77F, PO4), 1 pocket (best druggability 0.72). MolNFT v1 #78480 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3SAA
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
UniProt: O38732
Ligands: 77F, PO4
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease	protein	99	4% helix, 54% strand	O38732

Ligands and binding sites

77F · N-[(2S,3R)-4-{(cyclohexylmethyl)[(4-methoxyphenyl)sulfonyl]amino}-3-hydroxy-1-phenylbutan-2-yl]-3-hydroxybenzamide · ligand · chains A, B
PO4 · Phosphate ion · ion · 2 copies · chains A

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	0.72	0.83	35	77F

Interfaces

1 interface between chains.

A–B · 1834 Å² buried · 36 hydrogen bonds · protein-protein

Compared structures

3SAA · Crystal structure of Wild-type HIV-1 protease in complex With AF77 · 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 O38732
Elsewhere: RCSB PDB 3SAA · PDBe 3SAA · UniProt O38732

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.