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7M9K

HIV-1 Protease WT (NL4-3) in Complex with LR3-48

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 Residues7
Detailsbinding site for residue SO4 A 101
ChainResidue
AMET36
AASN37
AHOH204
AHOH242
BPRO39
BGLY40
BHOH104

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 102
ChainResidue
ALYS70
AHOH216
AHOH232
BPRO1
BLYS55
AGLY68
AHIS69

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 103
ChainResidue
APRO1
AHIS69
AHOH257

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 104
ChainResidue
ALYS7
AARG8
AHOH226

site_idAC5
Number of Residues26
Detailsbinding site for residue YWP A 105
ChainResidue
ATRP6
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APHE53
AVAL82
AHOH206
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BLEU76
BPRO81
BILE84
BGLN92
BHOH101
BHOH144

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_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

247947

PDB entries from 2026-01-21

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