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2R43

I50V HIV-1 protease in complex with an amino decorated pyrrolidine-based inhibitor

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 2701
ChainResidue
ATHR74
AASN88
BARG41

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 2702
ChainResidue
BTRP6
BLYS55

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 2703
ChainResidue
BTHR74
BASN88
BHOH3058

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE G3G B 2501
ChainResidue
AGLY27
AALA28
AASP30
AGLY48
AGLY49
AILE84
BASP25
BGLY27
BASP30
BGLY48
BGLY49
BPRO81
BILE84
BHOH3050
AASP25

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 2601
ChainResidue
AARG8
AHOH3041
AHOH3090
AHOH3146
BPHE53

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

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
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

221051

PDB entries from 2024-06-12

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