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2HB4

Structure of HIV Protease NL4-3 in an Unliganded State

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0044174cellular_componenthost cell endosome
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 101
ChainResidue
AHOH928
AHOH928
AHOH929
AHOH929
AHOH944
AHOH944
AHOH945

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGR A 906
ChainResidue
AGLY17
ALEU63
AGLU65
ALYS70
ALYS14
AGLY16

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGR A 907
ChainResidue
AASP29
AASP30
AVAL32
AHOH917

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGR A 908
ChainResidue
AILE72
AGLY73
ATHR74
APRO79
AASN88
ATHR91
AGLN92
AHOH941

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
ATHR26

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APRO1

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25

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PDB entries from 2025-07-02

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