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3EKX

Crystal structure of the wild-type HIV-1 protease with the inhibitor, Nelfinavir

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 Residues14
DetailsBINDING SITE FOR RESIDUE 1UN B 201
ChainResidue
AASP25
BILE50
BPRO81
BILE84
BHOH156
BHOH539
AGLY27
AASP29
AASP30
AGLY49
AILE84
BASP25
BGLY27
BGLY48

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 506
ChainResidue
ALYS7
AARG8
BARG87
BHOH508

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

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 2024-05-29

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