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3TL9

crystal structure of HIV protease model precursor/Saquinavir complex

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 Residues28
DetailsBINDING SITE FOR RESIDUE ROC A 401
ChainResidue
ATRP6
AILE50
ATHR80
APRO81
AILE84
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
AARG8
BILE47
BGLY48
BGLY49
BILE50
BTHR80
BPRO81
BVAL82
BILE84
BHOH1014
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 501
ChainResidue
AGLN18
AMET36
ASER37
BTHR12
BGLU65
BGLY68
BHOH1030

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
ATHR74
AASN88
BARG41

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 602
ChainResidue
BTHR74
BASN88
BHOH1013

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 611
ChainResidue
AASP60

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, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease
ChainResidueDetails
APHE0
BPHE-1

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

222415

PDB entries from 2024-07-10

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