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3O9E

Crystal Structure of wild-type HIV-1 Protease in complex with af60

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
AHOH150
AHOH166
BGLY16
BHOH130
BHOH150

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 101
ChainResidue
AGLU21
AASN83
AHOH128
AHOH158
ALYS20

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 102
ChainResidue
AMET36
AASN37
AHOH109
BPRO39
BGLY40
BHOH106

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 103
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH114
AHOH146
BPRO1

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 104
ChainResidue
AARG14
AGLY17
BPRO63

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE A60 A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH110
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BVAL82
BILE84
BHOH137

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

246704

PDB entries from 2025-12-24

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