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

---

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

Chain	Residue
X	HIS232
X	ASP269
X	HOH1373

---

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

---

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

---

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

Chain	Residue	Details
X	ARG65
X	TYR207
X	SER213
X	ARG333

---

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

Chain	Residue	Details
X	LYS149
X	ASN150
X	PHE152
X	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
X	HIS232
X	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
X	GLY248
X	GLU297
X	ARG449
X	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
X	LYS87
X	LYS523

---

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

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site_id	MCSA1
Number of Residues	8
Details	M-CSA 51

Chain

Residue

Details

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