1S2W

Crystal structure of phosphoenolpyruvate mutase in high ionic strength

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016853	molecular_function	isomerase activity
A	0032923	biological_process	organic phosphonate biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0050188	molecular_function	phosphoenolpyruvate mutase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 300

Chain	Residue
A	LYS116
A	ARG159
A	HOH453
A	HOH559
A	HOH561
A	HOH562

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255

Chain	Residue	Details
A	ASP58

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	ASP58

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	12
Details	M-CSA 271

Chain	Residue	Details
A	SER46	electrostatic stabiliser, hydrogen bond donor, steric role
A	GLY47	electrostatic stabiliser, steric role
A	LEU48	electrostatic stabiliser, hydrogen bond donor, steric role
A	ASP58	metal ligand, nucleofuge, nucleophile, promote heterolysis
A	ASP85	electrostatic stabiliser, hydrogen bond donor, metal ligand
A	ASP87	electrostatic stabiliser, hydrogen bond donor
A	GLU114	electrostatic stabiliser, hydrogen bond donor
A	LYS120	electrostatic stabiliser, promote heterolysis
A	ASN122	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
A	SER123	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
A	ARG159	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
A	HIS190	electrostatic stabiliser, hydrogen bond donor, promote heterolysis

---