1AQ2

PHOSPHOENOLPYRUVATE CARBOXYKINASE

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	0008152	biological_process	metabolic process
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 MN A 543

Chain	Residue
A	HOH548
A	LYS213
A	HIS232
A	ASP269
A	ATP541
A	HOH547

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 544

Chain	Residue
A	THR255
A	ASP268
A	ATP541
A	HOH546
A	HOH746
A	HOH747

---

site_id	AC3
Number of Residues	31
Details	BINDING SITE FOR RESIDUE ATP A 541

Chain	Residue
A	HIS232
A	LEU249
A	SER250
A	GLY251
A	THR252
A	GLY253
A	LYS254
A	THR255
A	THR256
A	ASP269
A	LYS288
A	ILE290
A	GLU297
A	ARG333
A	ARG449
A	ILE450
A	SER451
A	ILE452
A	THR455
A	PYR542
A	MN543
A	MG544
A	HOH546
A	HOH547
A	HOH548
A	HOH604
A	HOH617
A	HOH736
A	HOH746
A	HOH747
A	HOH748

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYR A 542

Chain	Residue
A	ARG65
A	LYS213
A	TYR286
A	ARG333
A	ATP541
A	HOH547
A	HOH548
A	HOH678
A	HOH679

---

site_id	ACT
Number of Residues	4
Details	ACTIVE SITE

Chain	Residue
A	ARG65
A	TYR207
A	LYS212
A	LYS213

---

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: BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:11724534

Chain	Residue	Details
A	ARG65
A	TYR207
A	LYS213
A	ARG333

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	LYS149
A	ASN150
A	PHE152
A	GLY283

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|Ref.21

Chain	Residue	Details
A	HIS232
A	ASP269

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, ECO:0000269|Ref.20, ECO:0000269|Ref.21

Chain	Residue	Details
A	GLY248
A	GLU297
A	ARG449
A	THR455

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	LYS87
A	LYS523

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Catalytic Information from CSA

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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