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4F73

Crystal Structure of active HIV-1 Protease in Complex with the N terminal product of CA-p2 cleavage site

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 Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 101
ChainResidue
AARG14
AHOH231
AHOH239
BARG14
BGLY16
BGLY17
BHOH110

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 102
ChainResidue
AVAL82
AASN83
AGLU21
AGLU34

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR CHAIN C OF N TERMINAL PRODUCT OF SUBSTRATE CA-P2
ChainResidue
AASP25
AGLY27
AASP29
AASP30
AILE47
AGLY48
AGLY49
AILE84
BARG8
BASP25
BILE50
BILE84
CHOH101
DVAL4
DLEU5

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR CHAIN D OF N TERMINAL PRODUCT OF SUBSTRATE CA-P2
ChainResidue
AASP25
AILE50
APRO81
AVAL82
BGLY27
BALA28
BASP29
BGLY48
BGLY49
CLEU5
CHOH101
DHOH101

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

224931

PDB entries from 2024-09-11

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