4P61

CHICKEN TRIOSEPHOSPHATE ISOMERASE WITH LOOP6 MUTATIONS, V167P AND W168E.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004807	molecular_function	triose-phosphate isomerase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006006	biological_process	glucose metabolic process
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0008929	molecular_function	methylglyoxal synthase activity
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0019242	biological_process	methylglyoxal biosynthetic process
A	0019563	biological_process	glycerol catabolic process
A	0019682	biological_process	glyceraldehyde-3-phosphate metabolic process
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0042803	molecular_function	protein homodimerization activity
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
A	0061621	biological_process	canonical glycolysis
B	0004807	molecular_function	triose-phosphate isomerase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006006	biological_process	glucose metabolic process
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0008929	molecular_function	methylglyoxal synthase activity
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0019242	biological_process	methylglyoxal biosynthetic process
B	0019563	biological_process	glycerol catabolic process
B	0019682	biological_process	glyceraldehyde-3-phosphate metabolic process
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0042803	molecular_function	protein homodimerization activity
B	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
B	0061621	biological_process	canonical glycolysis

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA163-GLY173

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Electrophile => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH

Chain	Residue	Details
A	HIS95
B	HIS95

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH

Chain	Residue	Details
A	GLU165
B	GLU165

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH

Chain	Residue	Details
A	ASN11
A	LYS13
B	ASN11
B	LYS13

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 324

Chain	Residue	Details
A	ASN11	electrostatic stabiliser
A	LYS13	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	HIS95	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU97	proton acceptor, proton donor, steric role
A	GLU165	activator, proton acceptor, proton donor
A	GLY171	electrostatic stabiliser
A	SER211	electrostatic stabiliser, hydrogen bond donor

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site_id	MCSA2
Number of Residues	7
Details	M-CSA 324

Chain	Residue	Details
B	ASN11	electrostatic stabiliser
B	LYS13	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	HIS95	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLU97	proton acceptor, proton donor, steric role
B	GLU165	activator, proton acceptor, proton donor
B	GLY171	electrostatic stabiliser
B	SER211	electrostatic stabiliser, hydrogen bond donor

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