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8DCH

Crystal Structure of a highly resistant HIV-1 protease Clinical isolate PR10x with GRL-0519 (tris-tetrahydrofuran as P2 ligand)

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 Residues33
Detailsbinding site for residue G52 A 201
ChainResidue
AASP25
APRO81
AVAL82
AHOH330
AHOH337
AHOH339
AHOH344
AHOH354
AHOH391
BARG8
BASP25
AGLY27
BGLY27
BALA28
BASP29
BASP30
BILE32
BGLN48
BGLY49
BILE50
BPRO81
BVAL82
AALA28
BHOH218
BHOH245
BHOH260
BHOH282
AASP29
AASP30
AILE32
AGLN48
AGLY49
AILE50

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 202
ChainResidue
AGLY73
ASER74
AASN88

site_idAC3
Number of Residues3
Detailsbinding site for residue CL B 101
ChainResidue
BGLY73
BSER74
BASN88

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL B 102
ChainResidue
BGLY16
BILE46
BPRO63
BHOH223
BHOH304

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTII
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
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

219869

PDB entries from 2024-05-15

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