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3HAW

Crystal structure of [L-Ala51/51']HIV-1 protease with reduced isostere MVT-101 inhibitor

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 Residues21
DetailsBINDING SITE FOR RESIDUE 2NC B 0
ChainResidue
AASP25
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
BVAL82
BHOH105
BHOH113
AGLY27
BHOH133
BHOH158
AALA28
AASP29
AGLY48
AGLY49
AVAL82
BASP25
BGLY27

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
AGLY16
AGLY17
APRO63
AHOH138
BARG14
BGLY17

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

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PDB entries from 2024-07-24

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