Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7LEA

HIV-1 Protease WT (NL4-3) in Complex with PU1 (LR3-46)

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 Residues5
Detailsbinding site for residue SO4 A 101
ChainResidue
AASN37
AHOH209
AHOH216
BPRO39
BGLY40

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 102
ChainResidue
AHIS69
ALYS70
AHOH242
BPRO1

site_idAC3
Number of Residues1
Detailsbinding site for residue SO4 A 103
ChainResidue
AGLN58

site_idAC4
Number of Residues20
Detailsbinding site for residue XUS A 104
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APHE53
AHOH208
AHOH210
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BPRO81
BHOH134
BHOH139

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

242842

PDB entries from 2025-10-08

PDB statisticsPDBj update infoContact PDBjnumon