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6PJM

HIV-1 Protease NL4-3 WT in Complex with LR2-35

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 Residues6
Detailsbinding site for residue SO4 A 101
ChainResidue
APRO1
ALYS55
AHOH277
BGLY68
BLYS70
BHOH248

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 102
ChainResidue
AHOH248
BLYS55
BLYS70
ALYS14
ALYS70
AHOH201

site_idAC3
Number of Residues20
Detailsbinding site for residue OQV B 101
ChainResidue
AASP25
AGLY27
AASP29
AGLY48
AGLY49
AILE50
AILE84
AHOH258
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BHOH235

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_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

218853

PDB entries from 2024-04-24

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