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3SA4

Crystal structure of wild-type HIV-1 protease in complex with AF72

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 Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
AARG14
AGLY16
AGLY17
AHOH144
AHOH150
AHOH161
AHOH162
BGLY16
BHOH133

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 101
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH179
BPRO1

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 102
ChainResidue
AMET36
AASN37
AHOH153
BPRO39
BGLY40
BHOH127

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 103
ChainResidue
ALYS20
AGLU21
AASN83
AHOH154

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE F72 B 200
ChainResidue
AASP25
AGLY27
AASP29
AASP30
AILE47
AGLY49
AILE50
AHOH114
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BVAL82
BILE84
BHOH136

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

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PDB entries from 2024-07-24

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