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3EKY

Crystal Structure of wild-type HIV protease in complex with the inhibitor, Atazanavir

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 Residues20
DetailsBINDING SITE FOR RESIDUE DR7 A 100
ChainResidue
AARG8
BTRP6
BARG8
BASP25
BGLY27
BALA28
BASP29
BGLY48
BGLY49
BILE50
BPRO81
AASP25
BILE84
AGLY27
AASP29
AGLY48
AGLY49
AILE50
AHOH508
AHOH580

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
AHOH582
BARG14
BILE15
BGLY16
BGLY17
BPRO63
BGLU65
BHOH537
BHOH590

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 502
ChainResidue
BLYS20
BGLU21
BASN83
BHOH548
BHOH579

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 503
ChainResidue
AGLY68
AHIS69
ALYS70
BPRO1
BLYS55
BHOH571

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 504
ChainResidue
APRO1
AARG57
AHIS69
AHOH555

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 2024-06-12

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