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1LV1

Crystal Structure Analysis of the non-active site mutant of tethered HIV-1 protease to 2.1A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33
AALA1022-LEU1033

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
ALEU1076

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
ALEU1076

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

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25

site_idMCSA1
Number of Residues3
DetailsM-CSA 175
ChainResidueDetails
AASP25hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ATHR26electrostatic stabiliser, transition state stabiliser
AGLY27electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-07-02

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