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3K4V

New crystal form of HIV-1 Protease/Saquinavir structure reveals carbamylation of N-terminal proline

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 901
ChainResidue
ALYS14
AILE15
AGLY16
AGLY17
AILE63
AGLU65
BGLY17

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS A 100
ChainResidue
AHOH1038
BLYS14
BILE15
BGLY16
BGLY17
BILE63
AGLY17
ADMS901

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ROC B 201
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49
AILE50
ATHR80
APRO81
AVAL82
AILE84
AHOH1041
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
BTHR80
BPRO81
BILE84
CTRP6

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 801
ChainResidue
BSER37

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS C 901
ChainResidue
CLYS14
CGLY17
CILE63

site_idAC6
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ROC D 201
ChainResidue
CARG8
CLEU23
CASP25
CGLY27
CALA28
CASP29
CASP30
CILE47
CGLY48
CILE50
CPRO81
CILE84
CHOH1001
DARG8
DLEU23
DASP25
DGLY27
DALA28
DASP29
DASP30
DVAL32
DGLY48
DGLY49
DILE50
DTHR80
DPRO81
DVAL82
DILE84
DHOH1039

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS D 901
ChainResidue
CGLY17
CDMS901
DLYS14
DILE15
DGLY16
DGLY17
DILE63

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
CALA22-ILE33
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
CASP25
DASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
CPHE99
DPHE99

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PDB entries from 2024-07-17

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