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6O5A

Crystal Structure of multi-drug resistant HIV-1 protease PR-S17 with a substrate analog p2-NC in P61

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0055036cellular_componentvirion membrane
B0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues29
Detailsbinding site for residue 2NC A 201
ChainResidue
AARG8
APRO81
ASER82
AILE84
AHOH312
AHOH336
AHOH340
AHOH357
BARG8
BASP25
BGLY27
AASP25
BALA28
BASP29
BASP30
BILE47
BVAL48
BGLY49
BILE50
BPRO81
BSER82
BILE84
AGLY27
AALA28
AASP29
AASP30
AILE47
AVAL48
AGLY49

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL B 101
ChainResidue
ATRP6
AGLN7
BASP29
BARG87
BHOH204
BHOH214

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

247536

PDB entries from 2026-01-14

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