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1D4K

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 Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AGLY68
AHIS69
ALYS70
BPRO1

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
APRO1
AHIS69

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE PI8 A 201
ChainResidue
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH321
BARG8
BASP25
BGLY27
BALA28
BASP29
BVAL32
BGLY48
BGLY49
BVAL82
BILE84
BHOH301
AARG8
AASP25
AGLY27

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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

222926

PDB entries from 2024-07-24

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