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1B6P

HIV-1 PROTEASE COMPLEXED WITH MACROCYCLIC PEPTIDOMIMETIC INHIBITOR 7

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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
AGLY68
ALYS70
BPRO101
BLYS155
BHOH375

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
APRO1
AARG57
AHIS69
AHOH352

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG14
AGLY17
AHOH350
AHOH367
BGLY116
BGLY117
BHOH314

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE PI7 A 201
ChainResidue
AARG8
AASP25
AGLY27
AASP29
AVAL32
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH301
AHOH377
BARG108
BASP125
BGLY127
BASP129
BASP130
BVAL132
BILE147
BGLY148
BGLY149
BILE150
BPRO181
BILE184

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

218500

PDB entries from 2024-04-17

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