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3OY4

Crystal Structure of HIV-1 L76V Protease in Complex with the Protease Inhibitor Darunavir.

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 Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
APRO1
ALYS55
BGLY68
BHIS69
BLYS70
BHOH178

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 101
ChainResidue
BARG87
ALYS7
AARG8
AHOH153

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 102
ChainResidue
BPRO1
BHIS69
BHOH176

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 103
ChainResidue
AGLY73
ATHR74
AASN88

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 104
ChainResidue
ATHR91
AGLN92
AHOH111
BGLY49
BPHE53

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 100
ChainResidue
AGLY16
AHOH131
AHOH164
BARG14
BGLY16
BGLY17
BHOH130

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 101
ChainResidue
BLYS20
BGLU21
BHOH165
BHOH167

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 102
ChainResidue
APRO39
AGLY40
BMET36
BASN37
BHOH175

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 103
ChainResidue
BLYS7
BARG8
BHOH118

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 104
ChainResidue
APRO63
BARG14
BGLY17
BLEU19
BPRO44
BHOH169
BHOH172

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT B 105
ChainResidue
BGLN58

site_idBC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 017 B 200
ChainResidue
AASP25
AGLY27
AALA28
AASP30
AVAL32
AGLY48
AGLY49
AVAL82
AILE84
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BILE50
BHOH111
BHOH125

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

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

218853

PDB entries from 2024-04-24

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