Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5YOJ

Structure of A17 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 Residues35
Detailsbinding site for residue 8Z0 A 301
ChainResidue
ATRP6
AGLY49
AILE50
APRO81
AVAL82
AHOH406
AHOH410
AHOH439
AHOH466
AHOH513
BLEU23
AARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL47
BGLY48
BGLY49
BILE50
BPHE53
ALEU23
BPRO81
BHOH238
BHOH306
BHOH337
BHOH344
BHOH364
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48

site_idAC2
Number of Residues11
Detailsbinding site for residue GOL B 101
ChainResidue
AGLN18
AMET36
ASER37
BTHR12
BILE13
BLYS14
BGLU65
BALA67
BGLY68
BHOH201
BHOH228

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL B 102
ChainResidue
BGLU35
BLYS55
BARG57
BVAL77
BGLY78
BHOH215
BHOH276

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTII
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, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease
ChainResidueDetails
AMET0
BMET0

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE99

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon