1DAZ

Structural and kinetic analysis of drug resistant mutants of HIV-1 protease

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	41
Details	BINDING SITE FOR RESIDUE 0Q4 D 601

Chain	Residue
C	TRP6
C	ILE45
C	MET46
C	ILE47
C	GLY48
C	GLY49
C	ILE50
C	PHE53
C	GLN58
C	PRO81
C	VAL82
C	ARG8
C	ILE84
D	HOH14
D	HOH49
D	ARG108
D	LEU123
D	ASP125
D	GLY127
D	ASP129
D	ASP130
D	VAL132
C	LEU23
D	MET146
D	ILE147
D	GLY148
D	GLY149
D	ILE150
D	PRO181
D	VAL182
D	ILE184
D	HOH261
D	HOH262
C	ASP25
D	HOH263
D	HOH387
C	GLY27
C	ALA28
C	ASP29
C	ASP30
C	VAL32

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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. ALLDTGADDTVI

Chain	Residue	Details
C	ALA22-ILE33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094

Chain	Residue	Details
C	THR26
D	THR126

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Cleavage; by viral protease => ECO:0000250

Chain	Residue	Details
C	PRO1
D	PRO101

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