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6OOT

HIV-1 Protease NL4-3 L89V, L90M Mutant in complex with darunavir

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 101
ChainResidue
ALYS7
AARG8
BARG8

site_idAC2
Number of Residues20
Detailsbinding site for residue 017 B 101
ChainResidue
AGLY49
AILE50
AILE84
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BPRO81
BVAL82
BILE84
BHOH209
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 B 102
ChainResidue
ATRP6
BARG87
BASN88
BHOH208

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues20
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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