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3DJK

Wild Type HIV-1 Protease with potent Antiviral inhibitor GRL-0255A

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 Residues1
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AASP60

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 511
ChainResidue
ATHR74
AASN88
BARG141

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 513
ChainResidue
BTHR174
BASN188

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE G55 B 401
ChainResidue
AASP30
AGLY48
AGLY49
APRO81
AILE84
BASP125
BGLY127
BALA128
BASP129
BASP130
BILE147
BGLY148
BGLY149
BILE150
BILE184
AASP25
AGLY27
AALA28

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

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
AASP25
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE199

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BTHR126
BASP125

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP125

229183

PDB entries from 2024-12-18

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