1K3C

Phosphoenolpyruvate carboxykinase in complex with ADP, AlF3 and Pyruvate

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 998

Chain	Residue
A	THR255
A	ADP541
A	HOH662
A	HOH753
A	HOH754
A	AF3999

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site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ADP A 541

Chain	Residue
A	THR252
A	GLY253
A	LYS254
A	THR255
A	THR256
A	LYS288
A	GLU297
A	THR441
A	ARG449
A	ILE450
A	SER451
A	THR455
A	HOH665
A	HOH681
A	HOH754
A	MG998
A	AF3999
A	LEU249
A	SER250
A	GLY251

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AF3 A 999

Chain	Residue
A	LYS213
A	HIS232
A	SER250
A	LYS254
A	ASP269
A	ARG333
A	ADP541
A	HOH662
A	MG998

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PYR A 542

Chain	Residue
A	ARG65
A	TYR207
A	LYS212
A	LYS213
A	TYR286
A	ARG333
A	HOH663
A	HOH774

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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
A	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
A	LYS254
A	ARG333
A	HIS232

---

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

Chain	Residue	Details
A	ARG333
A	HIS232

---

site_id	MCSA1
Number of Residues	8
Details	M-CSA 51

Chain	Residue	Details
A	ARG65	electrostatic stabiliser, increase electrophilicity
A	LYS213	metal ligand
A	HIS232	electrostatic stabiliser, hydrogen bond donor, metal ligand
A	SER250	steric role
A	LYS254	electrostatic stabiliser, hydrogen bond donor
A	THR255	metal ligand
A	ASP269	metal ligand
A	ARG333	electrostatic stabiliser, hydrogen bond donor

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