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3O9G

Crystal Structure of wild-type HIV-1 Protease in complex with af53

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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
AARG14
AGLY16
AGLY17
AHOH141
BGLY16
BHOH108
BHOH112
BHOH144

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 101
ChainResidue
AGLU21
AASN83
AHOH105
AHOH124
AHOH155
ALYS20

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 102
ChainResidue
AMET36
AASN37
AHOH104
BPRO39
BGLY40
BHOH131

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE F53 A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH119
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BVAL82
BILE84
BHOH102
BHOH145

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

220113

PDB entries from 2024-05-22

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