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3EM3

Crystal structure of amprenavir (APV) in complex with a drug resistant HIV-1 protease variant (I50L/A71V).

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 Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 501
ChainResidue
ALYS7
AARG8
ALEU10

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 502
ChainResidue
ALYS70
BPRO1

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 503
ChainResidue
ALYS20
AGLU21
AHOH554

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 504
ChainResidue
AHOH523
AHOH550
BGLY40
AASN37

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 478 B 200
ChainResidue
AASP25
AGLY27
AASP29
AASP30
AVAL32
AGLY49
ALEU50
AVAL82
AILE84
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BPRO81
BVAL82
BHOH524

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

221051

PDB entries from 2024-06-12

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