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3DCR

X-ray structure of HIV-1 protease and hydrated form of ketomethylene isostere inhibitor

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 Residues22
DetailsBINDING SITE FOR RESIDUE KVS B 101
ChainResidue
AARG8
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
BVAL82
BHOH257
AASP25
BHOH258
BHOH259
BHOH260
AGLY27
AALA28
AASP29
AGLY48
AGLY49
AHOH136
BASP25

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP25
BTHR26

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP25

237992

PDB entries from 2025-06-25

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