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4YE3

Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical Isolate PR20 with Inhibitor GRL-4410A

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 Y1 A 101
ChainResidue
AGLU34
AASP35
AGLU58
AASP60
AY1102
ACL103
ACL104
AHOH201
AHOH217

site_idAC2
Number of Residues8
Detailsbinding site for residue Y1 A 102
ChainResidue
AGLU34
AASP35
AGLU58
AASP60
AY1101
ACL103
ACL104
AHOH201

site_idAC3
Number of Residues6
Detailsbinding site for residue CL A 103
ChainResidue
AGLU34
AASP35
AGLU58
AY1101
AY1102
AHOH217

site_idAC4
Number of Residues8
Detailsbinding site for residue CL A 104
ChainResidue
AGLU34
AASP35
AGLU58
AASP60
AY1101
AY1102
AHOH201
AHOH228

site_idAC5
Number of Residues2
Detailsbinding site for residue CL A 105
ChainResidue
ALYS7
AARG8

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL A 106
ChainResidue
ATRP6
AHOH218
BARG87
BASP88

site_idAC7
Number of Residues4
Detailsbinding site for residue GOL A 107
ChainResidue
AARG87
AASP88
AHOH229
BTRP6

site_idAC8
Number of Residues29
Detailsbinding site for residue G04 B 201
ChainResidue
ALEU23
AASP25
AGLY27
AALA28
AASP29
AASN30
AILE32
AVAL47
AGLY48
AGLY49
AILE50
AVAL82
BASP25
BGLY27
BALA28
BASP29
BASN30
BILE32
BVAL47
BGLY48
BGLY49
BILE50
BVAL82
BHOH302
BHOH303
BHOH304
BHOH306
BHOH313
BHOH316

site_idAC9
Number of Residues8
Detailsbinding site for residue Y1 B 202
ChainResidue
BGLU34
BASP35
BGLU58
BASP60
BY1203
BCL204
BCL205
BHOH332

site_idAD1
Number of Residues7
Detailsbinding site for residue Y1 B 203
ChainResidue
BGLU34
BASP35
BGLU58
BASP60
BY1202
BCL204
BCL205

site_idAD2
Number of Residues6
Detailsbinding site for residue CL B 204
ChainResidue
BGLU34
BASP35
BGLU58
BY1202
BY1203
BHOH332

site_idAD3
Number of Residues7
Detailsbinding site for residue CL B 205
ChainResidue
BGLU34
BASP35
BGLU58
BASP60
BY1202
BY1203
BHOH334

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

218853

PDB entries from 2024-04-24

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