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2O4K

Crystal Structure of HIV-1 Protease (Q7K) in Complex with 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 Residues4
DetailsBINDING SITE FOR RESIDUE CL A 300
ChainResidue
ATHR74
AASN88
AHOH350
BARG41

site_idAC2
Number of Residues32
DetailsBINDING SITE FOR RESIDUE DR7 A 301
ChainResidue
AASP29
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH303
AHOH304
AHOH324
AHOH356
AHOH367
AHOH423
AHOH424
BARG8
BASP25
BGLY27
BALA28
BASP29
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH106
BHOH233
ATRP6
AARG8
AASP25
AGLY27
AALA28

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
ATHR26
BTHR26

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APRO1
BPRO1

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

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PDB entries from 2024-10-30

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