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3UHL

Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical Isolate PR20 in Complex with p2-NC substrate analog

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 101
ChainResidue
ALYS43
CLYS7
DARG57

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 102
ChainResidue
ALYS43
ALYS45
AMET46
DTRP42
DHOH202

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 2NC C 101
ChainResidue
CGLY27
CALA28
CASP29
CASN30
CILE32
CGLY48
CILE50
CPRO81
CHOH201
CHOH213
CHOH214
DASP25
DGLY27
DALA28
DASP29
DASN30
DILE32
DGLY48
DILE50
DTHR80
DVAL82
DHOH204
CASP25

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 102
ChainResidue
CLYS7
CARG8

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 101
ChainResidue
AARG8
APHE53
DPRO44
DLYS45
DMET46

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 Residues4
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP25
CASP25
DASP25

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99
CPHE99
DPHE99

221716

PDB entries from 2024-06-26

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