2PY7

Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys213Ser complexed with ATP-Mg2+-Mn2+

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0000166	molecular_function	nucleotide binding
X	0000287	molecular_function	magnesium ion binding
X	0003824	molecular_function	catalytic activity
X	0004611	molecular_function	phosphoenolpyruvate carboxykinase activity
X	0004612	molecular_function	phosphoenolpyruvate carboxykinase (ATP) activity
X	0005509	molecular_function	calcium ion binding
X	0005524	molecular_function	ATP binding
X	0005737	cellular_component	cytoplasm
X	0005829	cellular_component	cytosol
X	0006094	biological_process	gluconeogenesis
X	0016829	molecular_function	lyase activity
X	0016831	molecular_function	carboxy-lyase activity
X	0017076	molecular_function	purine nucleotide binding
X	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG X 998

Chain	Residue
X	THR255
X	HOH1012
X	HOH1022
X	HOH1040

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN X 999

Chain	Residue
X	HIS232
X	ASP269
X	HOH1373

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN X 1001

Chain	Residue
X	HIS104
X	HOH1488
X	ASP19
X	HIS21

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site_id	AC4
Number of Residues	28
Details	BINDING SITE FOR RESIDUE ATP X 541

Chain	Residue
X	HIS232
X	LEU249
X	SER250
X	GLY251
X	THR252
X	GLY253
X	LYS254
X	THR255
X	THR256
X	ASP269
X	LYS288
X	GLU297
X	ARG333
X	THR441
X	ARG449
X	ILE450
X	SER451
X	ILE452
X	THR455
X	HOH1012
X	HOH1022
X	HOH1040
X	HOH1100
X	HOH1130
X	HOH1230
X	HOH1327
X	HOH1375
X	HOH1384

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Functional Information from PROSITE/UniProt

site_id	PS00532
Number of Residues	16
Details	PEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWdDdGVfN

Chain	Residue	Details
X	LEU265-ASN280

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11724534","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys213Ser.","authors":["Delbaere L.T.J.","Cotelesage J.J.H.","Goldie H."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12837799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17475535","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8599762","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9406547","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of E. coli phosphoenolpyruvate carboxykinase (PEPCK) complexed with ATP, Mg2+, Mn2+, carbon dioxide and oxaloacetate.","authors":["Delbaere L.T.J.","Cotelesage J.J.H.","Goldie H."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys213Ser.","authors":["Delbaere L.T.J.","Cotelesage J.J.H.","Goldie H."]}}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

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 1aq2

Chain	Residue	Details
X	LYS254
X	ARG333
X	HIS232

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
X	ARG333
X	HIS232

---

site_id	MCSA1
Number of Residues	8
Details	M-CSA 51

Chain

Residue

Details

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