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Ligands
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0Q4 N-[(2r)-2-({N~5~-[amino(iminio)methyl]-L-ornithyl-L-valyl}amino)-4-methylpentyl]-L-phenylalanyl-L-alpha-glutamyl-L-alanyl-L-norleucinamide
Non-standard Residues
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Code : 1K1U   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Combining Mutations in HIV-1 Protease to Understand Mechanisms of Resistance
Release Data : 2002-07-10
Compound :
mol_id molecule chains synonym
1 PROTEASE RETROPEPSIN A,B Retropepsin, PR
ec: 3.4.23.16
mutation: Q7K, l33I, K45I, L63I, C67A, L90M, C95A
Source :
mol_id organism_scientific expression_system
1 Human immunodeficiency virus 1  (taxid:11676) Escherichia coli  (taxid:562)
Authors : Mahalingam, B., Boross, P., Wang, Y.-F., Louis, J.M., Fischer, C., Tozser, J., W Harrison, R., Weber, I.T.
Keywords : HIV-1 PROTEASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 1.55 Å )
Citation :

Combining mutations in HIV-1 protease to understand mechanisms of resistance.

Mahalingam, B.,Boross, P.,Wang, Y.F.  et al.
(2002)  Proteins  48 : 107 - 116

PubMed: 12012342
DOI: 10.1002/prot.10140

Chain : A, B
UniProt : P04587 (POL_HV1B5)
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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a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) 2.7.7.49 PROSITE- ProRule:PRU00405
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a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) 2.7.7.7 PROSITE- ProRule:PRU00405
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