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3NWX

X-ray structure of ester chemical analogue [O-Ile50,O-Ile50']HIV-1 protease complexed with KVS-1 inhibitor

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 SO4 A 502
ChainResidue
APRO1
BHIS69
BLYS70

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
AGLY73
ATHR74
AASN88
AGLN92
AHOH115

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE KVS B 100
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BHOH301
BHOH319
AARG8

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
AARG87
BLYS7
BARG8

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
BTHR12
BILE13
BARG14
BTRP42
BGLU65
BILE66
BABA67
BGLY68

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
ALEU5
ATRP6
BARG87
BTHR91
BHOH102

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
ChainResidueDetails
AASP25
BASP25

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

219140

PDB entries from 2024-05-01

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