1I2R

CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT S176A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004801	molecular_function	transaldolase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006098	biological_process	pentose-phosphate shunt
A	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
A	0016020	cellular_component	membrane
A	0016744	molecular_function	transketolase or transaldolase activity
B	0004801	molecular_function	transaldolase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006098	biological_process	pentose-phosphate shunt
B	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
B	0016020	cellular_component	membrane
B	0016744	molecular_function	transketolase or transaldolase activity

Functional Information from PROSITE/UniProt

site_id	PS00958
Number of Residues	18
Details	TRANSALDOLASE_2 Transaldolase active site. IlIKLAsTwQGIrAaEqL

Chain	Residue	Details
A	ILE129-LEU146

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site_id	PS01054
Number of Residues	9
Details	TRANSALDOLASE_1 Transaldolase signature 1. DATTNPSLI

Chain	Residue	Details
A	ASP31-ILE39

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00492","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"3140","lastPage":"3151","volume":"7","journal":"ChemCatChem","title":"Acid Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase.","authors":["Stellmacher L.","Sandalova T.","Leptihn S.","Schneider G.","Sprenger G.A.","Samland A.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/cctc.201500478"}]}}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Nucleophile; Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00492","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11298760","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"3140","lastPage":"3151","volume":"7","journal":"ChemCatChem","title":"Acid Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase.","authors":["Stellmacher L.","Sandalova T.","Leptihn S.","Schneider G.","Sprenger G.A.","Samland A.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/cctc.201500478"}]}}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27050126","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4S2C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
A	ASP17
A	GLU96
A	LYS132

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
B	ASP17
B	GLU96
B	LYS132

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 148

Chain	Residue	Details
A	ASP17	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU96	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LYS132	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	THR156	electrostatic stabiliser, hydrogen bond donor
A	PHE178	steric role

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 148

Chain	Residue	Details
B	ASP17	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLU96	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	LYS132	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	THR156	electrostatic stabiliser, hydrogen bond donor
B	PHE178	steric role

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