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3SA7

Crystal structure of wild-type HIV-1 protease in complex with AF55

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 Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 101
ChainResidue
AARG14
AGLY16
AGLY17
AHOH261
BGLY16
BHOH248
BHOH253

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 55A A 102
ChainResidue
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49
AILE50
AHOH204
BASP25
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BVAL82
BILE84
AASP25
AGLY27

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 101
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH247
BPRO1

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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