1FB7

CRYSTAL STRUCTURE OF AN IN VIVO HIV-1 PROTEASE MUTANT IN COMPLEX WITH SAQUINAVIR: INSIGHTS INTO THE MECHANISMS OF DRUG RESISTANCE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ROC A 100

Chain	Residue
A	ARG8
A	VAL48
A	GLY49
A	ILE50
A	ILE50
A	PRO81
A	PRO81
A	VAL82
A	VAL82
A	ILE84
A	ILE84
A	ASP25
A	HOH101
A	HOH101
A	HOH102
A	ASP25
A	GLY27
A	GLY27
A	ALA28
A	ASP29
A	ASP30
A	VAL48

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Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL

Chain	Residue	Details
A	ALA22-LEU33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000305|PubMed:33542150

Chain	Residue	Details
A	ASP25

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Cleavage; by viral protease => ECO:0000250

Chain	Residue	Details
A	PHE99

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 175

Chain	Residue	Details
A	ASP25	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	THR26	electrostatic stabiliser, transition state stabiliser
A	GLY27	electrostatic stabiliser, hydrogen bond donor

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