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4DQG

Crystal Structure of apo(G16C/L38C) 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 Residues6
DetailsBINDING SITE FOR RESIDUE HGU A 101
ChainResidue
AARG14
AILE15
ACYS16
AGLY17
AILE63
BARG14

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 102
ChainResidue
AASP25
AGOL103
BASP25

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 103
ChainResidue
AALA28
AASP29
AASP30
AGLY48
AGOL102

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE OXY A 104
ChainResidue
ACYS38

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 101
ChainResidue
BASP29
BASP30
BGLY48

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 102
ChainResidue
BPRO1
BARG57
BHIS69

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 103
ChainResidue
BLYS7
BARG8

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

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

249697

PDB entries from 2026-02-25

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