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3O9I

Crystal Structure of wild-type HIV-1 Protease in complex with af61

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 Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 100
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH131
BPRO1
BLYS55

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 101
ChainResidue
AHOH176
BPRO39
BGLY40
AMET36
AASN37
AHOH130

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
AARG14
AGLY16
AGLY17
AHOH103
BGLY16
BGLY17
BHOH155
BHOH177

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 101
ChainResidue
ALYS20
AGLU21
AASN83
AHOH140
AHOH147

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE A61 A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH149
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BILE84

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_FI2
Number of Residues20
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-03-25

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