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6PRF

HIV-1 Protease multiple drug resistant clinical isolate mutant PR20 with GRL-14213A

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 Residues10
Detailsbinding site for residue Y1 A 101
ChainResidue
AGLU34
AHOH278
AASP35
AGLU58
AASP60
AY1102
AY1103
AHOH207
AHOH257
AHOH271

site_idAC2
Number of Residues10
Detailsbinding site for residue Y1 A 102
ChainResidue
AASP35
AGLU58
AASP60
AY1101
AY1103
AHOH207
AHOH247
AHOH257
AHOH271
AHOH278

site_idAC3
Number of Residues8
Detailsbinding site for residue Y1 A 103
ChainResidue
AGLU34
AASP35
AGLU58
AASP60
AY1101
AY1102
AHOH271
AHOH278

site_idAC4
Number of Residues5
Detailsbinding site for residue Y1 A 104
ChainResidue
AGLU34
AASP35
AGLY78
APRO79
AHOH287

site_idAC5
Number of Residues35
Detailsbinding site for residue 7OA B 101
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASN30
AVAL47
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AHOH208
AHOH234
AHOH239
AHOH262
BARG8
BASP25
BGLY27
BALA28
BASP29
BASN30
BILE32
BVAL47
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BHOH201
BHOH202
BHOH211
BHOH228
BHOH242
BHOH287

site_idAC6
Number of Residues8
Detailsbinding site for residue Y1 B 102
ChainResidue
BGLU34
BASP35
BLYS45
BGLU58
BY1103
BY1105
BHOH241
BHOH279

site_idAC7
Number of Residues10
Detailsbinding site for residue Y1 B 103
ChainResidue
BGLU34
BASP35
BGLU58
BASP60
BY1102
BY1104
BY1105
BHOH214
BHOH224
BHOH241

site_idAC8
Number of Residues8
Detailsbinding site for residue Y1 B 104
ChainResidue
BASP35
BGLU58
BASP60
BY1103
BY1105
BHOH214
BHOH224
BHOH238

site_idAC9
Number of Residues8
Detailsbinding site for residue Y1 B 105
ChainResidue
BY1103
BY1104
BHOH241
BGLU34
BASP35
BGLU58
BASP60
BY1102

site_idAD1
Number of Residues7
Detailsbinding site for residue Y1 B 106
ChainResidue
BGLU34
BASP35
BGLY78
BPRO79
BHOH215
BHOH224
BHOH294

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADNTIF
ChainResidueDetails
AALA22-PHE33

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, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE99

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PDB entries from 2024-07-10

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