Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5UPZ

HIV-1 wild Type protease with GRL-0518A , an isophthalamide-derived P2-P3 ligand with the para-hydoxymethyl sulfonamide isostere as the P2' group

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 Residues25
Detailsbinding site for residue 8HD A 201
ChainResidue
AARG8
AGLY49
AVAL82
AILE84
AHOH302
AHOH333
AHOH348
AHOH375
BASP25
BGLY27
BASP29
ALEU23
BASP30
BGLY48
BGLY49
BILE50
BILE84
BHOH251
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AGLY48

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 202
ChainResidue
AASP60
AHOH322
AHOH355
AHOH371
AHOH373
AHOH395

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 203
ChainResidue
ATHR74
AASN88
AHOH324
AHOH417
BARG41

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 204
ChainResidue
ALYS45
AMET46
AHOH317
AHOH329
BGLN92
BCL103
BHOH237

site_idAC5
Number of Residues5
Detailsbinding site for residue NA B 101
ChainResidue
BASP60
BHOH217
BHOH224
BHOH281
BHOH313

site_idAC6
Number of Residues1
Detailsbinding site for residue CL B 102
ChainResidue
BTRP6

site_idAC7
Number of Residues4
Detailsbinding site for residue CL B 103
ChainResidue
AGOL204
BTHR74
BASN88
BHOH231

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL B 104
ChainResidue
ALEU5
AHOH319
AHOH328
BTHR91
BALA95
BHOH247

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 Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE99

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon