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1U8G

Crystal structure of a HIV-1 Protease in complex with peptidomimetic inhibitor KI2-PHE-GLU-GLU-NH2

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 Residues29
DetailsBINDING SITE FOR CHAIN I OF PEPTIDOMIMETIC INHIBITOR KI2-PHE-GLU-GLU-NH2
ChainResidue
AARG8
AGLY48
AGLY49
AILE50
APRO81
AVAL82
BARG8
BLEU23
BASP25
BGLY27
BALA28
ALEU23
BASP29
BASP30
BVAL32
BILE47
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
IHOH6
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AILE47

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 Residues138
DetailsDomain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

251422

PDB entries from 2026-04-01

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