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3O9F

Crystal Structure of wild-type HIV-1 Protease in complex with kd27

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 Residues18
DetailsBINDING SITE FOR RESIDUE K2D A 200
ChainResidue
AASP25
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BVAL82
BILE84
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH169

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 100
ChainResidue
AARG14
AGLY16
AGLY17
BGLY16
BHOH114
BHOH129
BHOH130
BHOH153

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 100
ChainResidue
ALYS20
AGLU21
AASN83
AHOH146

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 101
ChainResidue
AMET36
AASN37
AHOH105
BPRO39
BGLY40

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 102
ChainResidue
AGLY68
AHIS69
ALYS70
BPRO1

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

246704

PDB entries from 2025-12-24

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