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6O57

Crystal Structure of multi-drug resistant HIV-1 protease PR-S17 with a substrate analog p2-NC in P41

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 Residues3
Detailsbinding site for residue FMT A 101
ChainResidue
AGLN2
AARG57
AHOH228

site_idAC2
Number of Residues29
Detailsbinding site for residue 2NC B 201
ChainResidue
AILE47
AVAL48
AGLY49
AILE50
ATHR80
APRO81
ASER82
AILE84
AHOH203
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BVAL48
BGLY49
BILE50
BTHR80
BILE84
BHOH308
BHOH323
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30

site_idAC3
Number of Residues3
Detailsbinding site for residue FMT B 202
ChainResidue
BGLU21
BHOH322
BHOH333

site_idAC4
Number of Residues4
Detailsbinding site for residue FMT B 203
ChainResidue
APRO81
BVAL48
BVAL72
BGLN92

site_idAC5
Number of Residues5
Detailsbinding site for residue FMT B 204
ChainResidue
AVAL72
AGLN92
AHOH239
BPRO81
BHOH305

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

219140

PDB entries from 2024-05-01

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