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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASN339

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	ARG632

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING:

Chain	Residue	Details
A	VAL119
A	TYR126
A	VAL275
A	LYS312
A	ASN339
A	GLU428
A	PHE453
A	ARG456
A	SER537

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00641, ECO:0000269|PubMed:12930982

Chain	Residue	Details
A	SER618
A	ALA689

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 53

Chain	Residue	Details
A	CYS271	electrostatic stabiliser, hydrogen bond acceptor
A	ASP273	electrostatic stabiliser, hydrogen bond acceptor
A	ASN339	electrostatic stabiliser, hydrogen bond donor
A	GLU428	metal ligand
A	ARG456	metal ligand
A	ARG632	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---