Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3SA3

Crystal structure of wild-type HIV-1 protease in complex with AG23

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0044174cellular_componenthost cell endosome
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0044174cellular_componenthost cell endosome
B0055036cellular_componentvirion membrane
B0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 101
ChainResidue
ALYS70
BPRO1

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 102
ChainResidue
APRO1
AHIS69

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 103
ChainResidue
ALYS20
AGLU21
AASN83
AHOH227
AHOH236

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 23X B 101
ChainResidue
ALEU23
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AVAL82
AHOH201
BARG8
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BPRO81
BVAL82
BILE84
BHOH208

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 102
ChainResidue
BGLY73
BTHR74
BASN88
BGLN92

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

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon