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1T7I

The structural and thermodynamic basis for the binding of TMC114, a next-generation HIV-1 protease 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 Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
AARG14
BHOH634
AGLY16
AGLY17
AHOH621
AHOH626
AHOH632
BGLY16
BHOH613
BHOH617

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 502
ChainResidue
AARG87
AHOH616
AHOH684
AHOH689
BTRP6

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 503
ChainResidue
AMET36
AASN37
AHOH651
BPRO39
BGLY40
BHOH640
BHOH657

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 504
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH657
BPRO1

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 602
ChainResidue
ALYS20
AGLU21
AASN83
AHOH630
BHOH664

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 603
ChainResidue
BLYS7
BARG8
BHOH621

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 017 A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49
AILE50
AHOH604
AHOH653
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BTHR82

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
ALEU76
BLEU76

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
ALEU76
BLEU76

218853

PDB entries from 2024-04-24

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