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3NXN

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE KVS A 204
ChainResidue
AARG8
AARG112
AASP129
AGLY131
AALA132
AASP133
AASP134
AILE151
AGLY152
AGLY153
AVAL186
AASP25
AHOH301
AHOH303
AHOH333
AHOH334
AGLY27
AALA28
AASP29
AGLY48
AGLY49
AILE50
AVAL82

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ALEU114
AGLU125
AALA126
AVAL186
AASN187

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AARG14
AGLY16
AGLY17
AARG118
AHOH323
AHOH338
AHOH382

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
ALYS45
ANLE46
AHOH313

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
ATHR116
AILE117
AARG118
ATRP146
AGLU169
AILE170
AABA171
AGLY172

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33
AALA126-ILE137

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-09-24

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