1M6J

CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ENTAMOEBA HISTOLYTICA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004807	molecular_function	triose-phosphate isomerase activity
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0019563	biological_process	glycerol catabolic process
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
B	0004807	molecular_function	triose-phosphate isomerase activity
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016853	molecular_function	isomerase activity
B	0019563	biological_process	glycerol catabolic process
B	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00171
Number of Residues	11
Details	TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG

Chain	Residue	Details
A	ALA172-GLY182

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127

Chain	Residue	Details
A	HIS102
B	HIS102

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127

Chain	Residue	Details
A	GLU174
B	GLU174

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site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q07412

Chain	Residue	Details
A	ASN11
B	GLY241
A	LYS13
A	GLY180
A	LEU239
A	GLY241
B	ASN11
B	LYS13
B	GLY180
B	LEU239

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