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3GI4

Crystal structure of protease inhibitor, KB60 in complex with wild type HIV-1 protease

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 Residues21
DetailsBINDING SITE FOR RESIDUE K60 A 200
ChainResidue
AASP25
AHOH117
BARG8
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BPRO81
BVAL82
AGLY27
BILE84
BACT503
AALA28
AASP29
AGLY48
AGLY49
AILE50
APHE53
AHOH101

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
AARG14
AGLY16
AGLY17
AHOH150
AHOH173
BGLY16
BHOH107
BHOH178

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 502
ChainResidue
ALYS20
AGLU21
AASN83
AHOH134
AHOH191

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 504
ChainResidue
AASN37
AHOH141
AHOH187
BPRO39
BGLY40

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 503
ChainResidue
AK60200
BARG8

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

226707

PDB entries from 2024-10-30

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