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1D4L

HIV-1 PROTEASE COMPLEXED WITH A MACROCYCLIC PEPTIDOMIMETIC 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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH353
BPRO1
BLYS55

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AHOH363
AHOH417
APRO1
AABA67
AHIS69

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG14
BARG14
BGLY16
BGLY17

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE PI9 A 201
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH301
BARG8
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BVAL82
BILE84

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
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AGLY78
BGLY78

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AGLY78
BGLY78

219869

PDB entries from 2024-05-15

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