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4EJK

HIV Protease (PR) dimer in closed form with pepstatin in active site and fragment 1F1-N in the outside/top of flap

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 Residues10
DetailsBINDING SITE FOR RESIDUE IOP A 101
ChainResidue
ATRP42
BTRP6
APRO44
ALYS45
ALYS55
AVAL56
AGLN92
AILE93
AGLY94
AHOH207

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR CHAIN N OF PEPSTATIN
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49
AILE50
AILE84
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BHOH208
BHOH242
NHOH101

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

237735

PDB entries from 2025-06-18

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