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3UF3

Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical isolate PR20

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 Y1 A 201
ChainResidue
AGLU34
AGLU58
AHOH439
AHOH440
AHOH458

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE Y1 B 202
ChainResidue
AHOH437
BHOH436
BHOH438

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 210
ChainResidue
BGLU65
BALA67
BGLY68
BHOH463
BLEU19

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADNTIF
ChainResidueDetails
AALA22-PHE33

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

222415

PDB entries from 2024-07-10

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