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7MAH

HIV-1 Protease (I84V) in Complex with PU4 (LR2-78)

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 Residues9
Detailsbinding site for residue SO4 B 101
ChainResidue
ALYS14
AGLY17
BLYS14
BILE15
BGLY16
BGLY17
BHOH202
BHOH203
BHOH217

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 101
ChainResidue
ALYS7
AARG8
AHOH220
BHOH263

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 102
ChainResidue
AHIS69
ALYS70
AHOH209
BPRO1

site_idAC4
Number of Residues26
Detailsbinding site for residue XVM A 103
ChainResidue
ATRP6
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APHE53
AVAL82
AHOH214
AHOH217
AHOH235
BASP25
BGLY27
BALA28
BASP30
BVAL32
BILE47
BGLY48
BGLY49
BPRO81
BVAL82
BGLN92
BHOH243

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
BALA22-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
BASP25
AASP25

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

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PDB entries from 2024-10-16

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