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1TCW

SIV PROTEASE COMPLEXED WITH INHIBITOR SB203386

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 Residues14
DetailsBINDING SITE FOR RESIDUE IM1 A 400
ChainResidue
AALA28
AHOH505
AHOH507
BARG8
BLEU23
BILE50
AASP29
AASP30
AILE32
AILE46
AVAL47
AGLY48
AGLY49
AILE84

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE IM1 B 600
ChainResidue
AARG8
AILE50
APRO81
AHOH507
AHOH515
BGLY27
BALA28
BASP29
BASP30
BVAL47
BGLY48
BHOH522
BHOH535

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLLDTGADDSIV
ChainResidueDetails
AVAL22-VAL33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE3
ALEU99
BPHE3
BLEU99

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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