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3HAU

Crystal structure of chemically synthesized 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 Residues26
DetailsBINDING SITE FOR RESIDUE 2NC A 0
ChainResidue
AASP25
AVAL82
AHOH101
AHOH107
AHOH111
AHOH117
AHOH142
BARG8
BLEU23
BASP25
BGLY27
AGLY27
BALA28
BASP29
BGLY48
BGLY49
BPRO81
BVAL82
BHOH119
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49
AILE50

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AARG14
BARG14
BPRO63
BHOH118

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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