1Y8B

Solution NMR-Derived Global Fold of Malate Synthase G from E.coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0004474	molecular_function	malate synthase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006097	biological_process	glyoxylate cycle
A	0006099	biological_process	tricarboxylic acid cycle
A	0009436	biological_process	glyoxylate catabolic process
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00589
Number of Residues	16
Details	PTS_HPR_SER PTS HPR domain serine phosphorylation site signature. EIsLHgRSLLFIRnVG

Chain	Residue	Details
A	GLU326-GLY341

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor"}

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor"}

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site_id	SWS_FT_FI3
Number of Residues	11
Details	Binding site: {}

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"HAMAP-Rule","id":"MF_00641","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12930982","evidenceCode":"ECO:0000269"}]}

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1d8c

Chain	Residue	Details
A	ARG338
A	GLU272
A	ASP270
A	ASP631

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site_id	MCSA1
Number of Residues	6
Details	M-CSA 53

Chain	Residue	Details
A	ASP270	electrostatic stabiliser, hydrogen bond acceptor
A	GLU272	electrostatic stabiliser, hydrogen bond acceptor
A	ARG338	electrostatic stabiliser, hydrogen bond donor
A	GLU427	metal ligand
A	ASP455	metal ligand
A	ASP631	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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