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

3SAA

Crystal structure of Wild-type HIV-1 protease in complex With AF77

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0055036cellular_componentvirion membrane
B0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
AARG14
AGLY16
AGLY17
AHOH134
AHOH154
BGLY16
BHOH130
BHOH131

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 101
ChainResidue
AHIS69
ALYS70
AHOH161
BPRO1
BLYS55
AGLY68

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 77F B 200
ChainResidue
AASP25
AGLY27
AASP29
AASP30
AILE47
AGLY49
AILE50
AILE84
AHOH152
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BVAL82
BILE84
BHOH103

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

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon