6ASM

E. coli phosphoenolpyruvate carboxykinase G209S K212C mutant bound to thiosulfate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
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	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	29
Details	binding site for residue ATP A 701

Chain	Residue
A	HIS232
A	ASP269
A	LYS288
A	GLU297
A	ARG333
A	THR441
A	ARG449
A	ILE450
A	SER451
A	ILE452
A	THR455
A	LEU249
A	MG702
A	MN703
A	HOH822
A	HOH831
A	HOH839
A	HOH899
A	HOH912
A	HOH914
A	HOH950
A	HOH1041
A	SER250
A	GLY251
A	THR252
A	GLY253
A	LYS254
A	THR255
A	THR256

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 702

Chain	Residue
A	THR255
A	ATP701
A	HOH831
A	HOH839
A	HOH899

---

site_id	AC3
Number of Residues	5
Details	binding site for residue MN A 703

Chain	Residue
A	HIS232
A	ASP269
A	ATP701
A	HOH826
A	HOH1108

---

site_id	AC4
Number of Residues	7
Details	binding site for residue BTB A 705

Chain	Residue
A	PRO96
A	LEU97
A	SER98
A	THR101
A	GLN183
A	HOH847
A	HOH879

---

site_id	AC5
Number of Residues	8
Details	binding site for residue THJ A 706

Chain	Residue
A	ARG65
A	SER209
A	LYS213
A	ARG333
A	PHE413
A	HOH826
A	HOH1022
A	HOH1043

---

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

---

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

---

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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