4BI7

CRYSTAL STRUCTURE OF A MUTANT (C202A) OF TRIOSEPHOSPHATE ISOMERASE FROM GIARDIA LAMBLIA COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID

Replaces:  2YC7

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	13
Details	BINDING SITE FOR RESIDUE PGA A 401

Chain	Residue
A	ASN11
A	GLY238
A	HOH2013
A	HOH2172
A	HOH2174
A	LYS13
A	HIS96
A	GLU170
A	SER174
A	ILE175
A	GLY176
A	SER216
A	GLY237

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 1258

Chain	Residue
A	ILE52
A	ASN55
A	LEU60
A	ARG61
A	ILE62
A	HOH2055
A	HOH2069
A	HOH2107
A	HOH2192

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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	Active site: {"description":"Electrophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10127","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10127","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10127","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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