4BI6

CRYSTAL STRUCTURE OF A TRIPLE MUTANT (A198V, C202A AND C222N) OF TRIOSEPHOSPHATE ISOMERASE FROM GIARDIA LAMBLIA. COMPLEXED WITH 2- PHOSPHOGLYCOLIC ACID

Replaces:  2YC6

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	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	0019563	biological_process	glycerol catabolic process
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PGA A 401

Chain	Residue
A	ASN11
A	LEU235
A	GLY237
A	GLY238
A	HOH2013
A	HOH2204
A	HOH2206
A	HOH2220
A	LYS13
A	HIS96
A	GLU170
A	SER174
A	ILE175
A	GLY176
A	GLY215
A	SER216

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA168-GLY178

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127

Chain	Residue	Details
A	HIS96

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127

Chain	Residue	Details
A	GLU170

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10127

Chain	Residue	Details
A	ASN11
A	LYS13

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