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6DGY

Crystal structure of HIV-1 Protease NL4-3 WT in complex with UMass1

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 Residues6
Detailsbinding site for residue SO4 A 101
ChainResidue
AMET36
AASN37
AHOH203
AHOH229
BPRO39
BGLY40

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 102
ChainResidue
AHOH204
AHOH246
BPRO1
AGLY68
AHIS69
ALYS70

site_idAC3
Number of Residues17
Detailsbinding site for residue K13 A 103
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH224
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BPRO81
BHOH123

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
BALA22-LEU33

247536

PDB entries from 2026-01-14

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