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7LE2

HIV-1 Protease WT (NL4-3) in Complex with UMass4

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 Residues4
Detailsbinding site for residue SO4 B 101
ChainResidue
BLYS20
BGLU21
BASN83
BHOH201

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 B 102
ChainResidue
BGLY73
BTHR74
BASN88
BHOH213

site_idAC3
Number of Residues18
Detailsbinding site for residue K20 A 101
ChainResidue
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH220
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BPRO81
BILE84
BHOH236
AASP25

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 102
ChainResidue
ALYS7
AARG8
AHOH208

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 103
ChainResidue
AMET36
AASN37
BPRO39
BGLY40

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

250359

PDB entries from 2026-03-11

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