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7M9H

HIV-1 Protease (I84V) in Complex with LR2-20

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 Residues5
Detailsbinding site for residue SO4 B 101
ChainResidue
BLYS20
BGLU21
BGLU34
BASN83
BHOH255

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 B 102
ChainResidue
BGLY16
BGLY17
BHOH201
BHOH216
ALYS14
AGLY17
BLYS14
BILE15

site_idAC3
Number of Residues21
Detailsbinding site for residue NJG A 101
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AHOH212
AHOH214
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BPRO81
BHOH203

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 102
ChainResidue
AMET36
AASN37
AHOH202
BPRO39
BGLY40

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 103
ChainResidue
AHIS69
ALYS70
AHOH251
BPRO1

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 104
ChainResidue
ALYS7
AARG8
AHOH216
BHOH265

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 2024-06-12

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