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1DAZ

Structural and kinetic analysis of drug resistant mutants of HIV-1 protease

Functional Information from GO Data
ChainGOidnamespacecontents
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues41
DetailsBINDING SITE FOR RESIDUE 0Q4 D 601
ChainResidue
CTRP6
CILE45
CMET46
CILE47
CGLY48
CGLY49
CILE50
CPHE53
CGLN58
CPRO81
CVAL82
CARG8
CILE84
DHOH14
DHOH49
DARG108
DLEU123
DASP125
DGLY127
DASP129
DASP130
DVAL132
CLEU23
DMET146
DILE147
DGLY148
DGLY149
DILE150
DPRO181
DVAL182
DILE184
DHOH261
DHOH262
CASP25
DHOH263
DHOH387
CGLY27
CALA28
CASP29
CASP30
CVAL32

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
CALA22-ILE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues138
DetailsDomain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
DTHR126
DASP125
CASP25
CTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
CASP25
DASP125

246031

PDB entries from 2025-12-10

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