MolNFT v1 · #62662 · protein

Crystal structure of amprenavir (apv) in complex with a drug resistant HIV-1 protease variant (I50L/A71V).

3EM3: “Crystal structure of amprenavir (apv) in complex with a drug resistant HIV-1 protease variant (I50L/A71V).”. X-ray diffraction, 1 ligand (478), 1 pocket (best druggability 0.72). MolNFT v1 #62662 on GenesisL1: 3D structure, binding…

PDB: 3EM3
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: P03369
Ligands: 478
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 (EC 3.4.23.16)	protein	99	4% helix, 54% strand	P03369

Ligands and binding sites

478 · {3-[(4-amino-benzenesulfonyl)-isobutyl-amino]-1-benzyl-2-hydroxy-propyl}-carbamic acid tetrahydro-furan-3-yl ester · ligand · chains A, B
ACT · Acetate ion · additive · 4 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	338	0.72	0.84	36	478

Interfaces

1 interface between chains.

A–B · 1839 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

3EM3 · Crystal structure of amprenavir (APV) in complex with a drug resistant HIV-1 protease… · 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 P03369
Elsewhere: RCSB PDB 3EM3 · PDBe 3EM3 · UniProt P03369

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