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1B6M

HIV-1 PROTEASE COMPLEXED WITH MACROCYCLIC PEPTIDOMIMETIC INHIBITOR 6

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
AHIS69
ALYS70
APHE99
BPRO101
BLYS155
BHOH359

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AHOH383
APRO1
AARG57
AHIS69

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG14
AGLY17
AHOH379
BARG114
BILE115
BGLY116
BGLY117
BHOH315

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PI6 B 201
ChainResidue
AARG8
AASP25
AGLY27
AGLY48
AGLY49
APRO81
AVAL82
BASP125
BGLY127
BALA128
BASP129
BVAL132
BGLY148
BILE150
BPRO181
BILE184
BHOH301
BHOH343

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
BGLY178

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AGLY78
BGLY178

218853

PDB entries from 2024-04-24

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