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1B6K

HIV-1 PROTEASE COMPLEXED WITH MACROCYCLIC PEPTIDOMIMETIC INHIBITOR 5

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
AGLY68
AHIS69
ALYS70
BPRO101
BLYS155
BHOH384
BHOH389

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AHIS69
AHOH391
APRO1
AARG57

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG14
AHOH357
BARG114
BGLY116
BGLY117
BHOH392

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PI5 A 201
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AGLY48
AGLY49
APRO81
AHOH301
AHOH317
AHOH382
AHOH395
BARG108
BASP125
BGLY127
BALA128
BASP129
BGLY148
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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BTHR126
BASP125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP125

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PDB entries from 2024-05-01

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