Structure of PDB 1hpx Chain B Binding Site BS01

Receptor Information

>1hpx Chain B (length=99) Species: 11676 (Human immunodeficiency virus 1)

PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGI
GGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF

Ligand information

• Ligand ID: KNI
• InChI: InChI=1S/C33H41N5O6S2/c1-33(2,3)37-31(42)26-19-46-20-38(26)32(43)29(40)24(15-21-9-6-5-7-10-21)36-30(41)25(18-45-4)35-28(39)17-44-27-12-8-11-22-16-34-14-13-23(22)27/h5-14,16,24-26,29,40H,15,17-20H2,1-4H3,(H,35,39)(H,36,41)(H,37,42)/t24-,25-,26-,29-/m0/s1
• InChIKey: NJBBLOIWMSYVCQ-VZTVMPNDSA-N
• SMILES:
  CACTVS 3.370: CSC[CH](NC(=O)COc1cccc2cnccc12)C(=O)N[CH](Cc3ccccc3)[CH](O)C(=O)N4CSC[CH]4C(=O)NC(C)(C)C
  OpenEye OEToolkits 1.7.0: CC(C)(C)NC(=O)[C@@H]1CSCN1C(=O)[C@H]([C@H](Cc2ccccc2)NC(=O)[C@H](CSC)NC(=O)COc3cccc4c3ccnc4)O
  OpenEye OEToolkits 1.7.0: CC(C)(C)NC(=O)C1CSCN1C(=O)C(C(Cc2ccccc2)NC(=O)C(CSC)NC(=O)COc3cccc4c3ccnc4)O
  CACTVS 3.370: CSC[C@H](NC(=O)COc1cccc2cnccc12)C(=O)N[C@@H](Cc3ccccc3)[C@H](O)C(=O)N4CSC[C@H]4C(=O)NC(C)(C)C
  ACDLabs 12.01: O=C(NC(C)(C)C)C4N(C(=O)C(O)C(NC(=O)C(NC(=O)COc2c1ccncc1ccc2)CSC)Cc3ccccc3)CSC4
• Formula: C33 H41 N5 O6 S2
• Name: (4R)-N-tert-butyl-3-[(2S,3S)-2-hydroxy-3-({N-[(isoquinolin-5-yloxy)acetyl]-S-methyl-L-cysteinyl}amino)-4-phenylbutanoyl]-1,3-thiazolidine-4-carboxamide;
  KNI-272;
  (N-TERT-BUTYL-THIOPROLINE)-(5-ISOQUINOLYLOXYACETYL-METHYLTHIOALANINE)-ALLOPHENYLNORSTATINE
• ChEMBL: CHEMBL414640
• PDB chain: 1hpx Chain B Residue 900

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1hpx Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): D25 G27 A28 D29 D30 V32 G48 G49 I50
• Binding residue (residue number reindexed from 1): D25 G27 A28 D29 D30 V32 G48 G49 I50
• Annotation score: 1
• Binding affinity: MOAD: Ki=5.5pM
  PDBbind-CN: -logKd/Ki=11.26,Ki=5.5pM

Enzymatic activity

• Catalytic site (original residue number in PDB): D25 T26 G27
• Catalytic site (residue number reindexed from 1): D25 T26 G27
• Enzyme Commision number: 2.7.7.-
  2.7.7.49: RNA-directed DNA polymerase.
  2.7.7.7: DNA-directed DNA polymerase.
  3.1.-.-
  3.1.13.2: exoribonuclease H.
  3.1.26.13: retroviral ribonuclease H.
  3.4.23.16: HIV-1 retropepsin.

Gene Ontology

Molecular Function

• GO:0004190 aspartic-type endopeptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:1hpx, PDBe:1hpx, PDBj:1hpx
• PDBsum: 1hpx
• PubMed: 8590019
• UniProt: P03367|POL_HV1BR Gag-Pol polyprotein (Gene Name=gag-pol)