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6B36

Crystal Structure of HIV Protease complexed with (S)-N-(3-fluoro-2-(2-(1-(phenylsulfonyl)piperazin-2-yl)ethyl)phenyl)-3,3-bis(4-fluorophenyl)propanamide

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 Residues4
Detailsbinding site for residue CL A 101
ChainResidue
ATHR74
AASN88
AHOH261
BARG41

site_idAC2
Number of Residues20
Detailsbinding site for residue CKD B 101
ChainResidue
AILE50
AVAL82
AILE84
AHOH233
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BILE84
BHOH210
AARG8
AASP25
AGLY27
AGLY48
AGLY49

site_idAC3
Number of Residues3
Detailsbinding site for residue CL B 102
ChainResidue
BTHR74
BASN88
BHOH237

site_idAC4
Number of Residues1
Detailsbinding site for residue CL B 103
ChainResidue
BTRP6

site_idAC5
Number of Residues3
Detailsbinding site for residue CL B 104
ChainResidue
BTHR12
BCYS67
BHOH264

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
BASP25

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

222415

PDB entries from 2024-07-10

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