Brand  (β version)

PDB ID: 1KZK

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Ligands
Code Name Style Show Link
CL Chloride ion PoSSuM
EDO 1,2-ethanediol PoSSuM
JE2 (4r)-3-{(2s,3s)-2-hydroxy-3-[(3-hydroxy-2-methylbenzoyl)amino]-4-phenylbutanoyl}-5,5-dimethyl-N-(2-methylbenzyl)-1,3-thiazolidine-4-carboxamide PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1KZK   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : JE-2147-HIV Protease Complex
Release Data : 2002-04-03
Compound :
mol_id molecule chains synonym
1 Protease A,B Retropepsin
ec: 3.4.23.16
mutation: Q7K, K14R, S37N, R41K, L63P, I64V
Source :
mol_id organism_scientific expression_system
1 Human immunodeficiency virus  (taxid:12721) Escherichia coli  (taxid:562)
expression_system_vector_type: Plasmid
expression_system_plasmid: pTacTac
Authors : Reiling, K.K., Endres, N.F., Dauber, D.S., Craik, C.S., Stroud, R.M.
Keywords : HIV Protease Complex, Anisotropic Displacement Parameters, Viral protein, hydrolase, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 1.09 Å )
Citation :

Anisotropic Dynamics of the JE-2147-HIV Protease Complex: Drug Resistance and Thermodynamic Binding Mode Examined in a 1.09 A Structure

Reiling, K.K.,Endres, N.F.,Dauber, D.S.  et al.
(2002)  Biochemistry  41 : 4582 - 4594

PubMed: 11926820
DOI: 10.1021/bi011781z

Structure-Activity Relationship of Small-Sized HIV Protease Inhibitors Containing Allophenylnorstatine

Mimoto, T.,Kato, R.,Takaku, H.  et al.
(1999)  J.Med.Chem.  42 : 1789 - 1802

DOI: 10.1021/jm980637h

Reaction

Chain : A, B
UniProt : P03369 (POL_HV1A2)
Reaction: EC: Evidence:
Physiological Direction:
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro. 3.4.23.16 PROSITE-ProRule:PRU00275
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Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus. 3.1.26.13 ECO:0000250
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. 3.1.13.2 ECO:0000250
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 2.7.7.49 PROSITE-ProRule:PRU00405
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 2.7.7.7 PROSITE-ProRule:PRU00405
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Cofactor: Evidence: Note:
Mg(2+) ECO:0000250
Binds 2 magnesium ions for reverse transcriptase polymerase activity.
Mg(2+) ECO:0000250
Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.
Mg(2+) ECO:0000250
Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.