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5YOK

Structure of HIV-1 Protease in Complex with Inhibitor KNI-1657

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 Residues44
Detailsbinding site for residue 8Z0 A 101
ChainResidue
ATRP6
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH202
AHOH207
AHOH212
AHOH220
AHOH247
AARG8
AHOH248
AHOH282
AHOH288
AHOH308
AHOH367
AHOH442
AHOH499
BARG8
BLEU23
BASP25
ALEU23
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
AASP25
BILE84
BHOH210
BHOH354
BHOH399
BHOH429
AGLY27
AALA28
AASP29
AASP30
AGLY48

site_idAC2
Number of Residues12
Detailsbinding site for residue GOL B 101
ChainResidue
AGLN18
AMET36
ASER37
BTHR12
BILE13
BLYS14
BLEU19
BGLU65
BALA67
BGLY68
BHOH232
BHOH260

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL B 102
ChainResidue
AHOH407
BGLU35
BLYS55
BARG57
BVAL77
BGLY78
BHOH206
BHOH278

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 Residues4
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AMET0
APHE99
BMET0
BPHE99

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PDB entries from 2024-07-17

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