1TRE

THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI DETERMINED AT 2.6 ANGSTROM RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004807	molecular_function	triose-phosphate isomerase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016020	cellular_component	membrane
A	0016853	molecular_function	isomerase activity
A	0019563	biological_process	glycerol catabolic process
A	0042802	molecular_function	identical protein binding
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
B	0004807	molecular_function	triose-phosphate isomerase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016020	cellular_component	membrane
B	0016853	molecular_function	isomerase activity
B	0019563	biological_process	glycerol catabolic process
B	0042802	molecular_function	identical protein binding
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	ALA167-GLY177

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147

Chain	Residue	Details
A	HIS97
B	HIS97

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147

Chain	Residue	Details
A	GLU169
B	GLU169

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147

Chain	Residue	Details
A	ASN11
A	GLY175
A	SER214
A	GLY235
B	ASN11
B	GLY175
B	SER214
B	GLY235

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