PDBsum entry 3s54

Hydrolase/hydrolase inhibitor

PDB id: 3s54

Contents

Protein chains

99 a.a.

Ligands

017

GOL

ACT

Metals

_CL ×2

_NA

Waters ×161

PDB id:

3s54

Name:

Hydrolase/hydrolase inhibitor

Title:

HIV-1 protease triple mutants v32i, i47v, v82i with antiviral drug darunavir in space group p21212

Structure:

Protease. Chain: a, b. Fragment: residues 500-598. Engineered: yes. Mutation: yes

Source:

Human immunodeficiency virus 1. Organism_taxid: 11676. Gene: pol. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.42Å R-factor: 0.157 R-free: 0.208

Authors:

Y.-F.Tie,Y.-F.Wang,I.T.Weber

Key ref:

Y.Tie et al. (2012). Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors. Protein Sci, 21, 339-350. PubMed id: 22238126

Date:

20-May-11 Release date: 21-Mar-12

Protein chains

Q7SSI0  (Q7SSI0_9HIV1) -  Protease (Fragment) from Human immunodeficiency virus 1

Seq: 99 a.a.

Struc: 99 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.23.16 - HIV-1 retropepsin.
• Reaction: Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.

Protein Sci 21:339-350 (2012)

PubMed id: 22238126

Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors.

Y.Tie, Y.F.Wang, P.I.Boross, T.Y.Chiu, A.K.Ghosh, J.Tozser, J.M.Louis, R.W.Harrison, I.T.Weber.

ABSTRACT

No abstract given.