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7LEC

HIV-1 Protease WT (NL4-3) in Complex with PU3 (LR3-69)

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 Residues22
Detailsbinding site for residue XVP B 101
ChainResidue
AASP25
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BPRO81
BGLN92
AGLY27
BHOH203
BHOH211
BHOH234
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AVAL82

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 101
ChainResidue
AGLN18
AMET36
AASN37
BPRO39
BGLY40

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 102
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH203
BPRO1

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
BALA22-LEU33

Functional Information from SwissProt/UniProt
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

239803

PDB entries from 2025-08-06

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