3GP5

Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with 3-phosphoglyceric acid and vanadate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004619	molecular_function	phosphoglycerate mutase activity
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0046538	molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
B	0003824	molecular_function	catalytic activity
B	0004619	molecular_function	phosphoglycerate mutase activity
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016853	molecular_function	isomerase activity
B	0016868	molecular_function	intramolecular phosphotransferase activity
B	0046538	molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PG6 A 250

Chain	Residue
A	ILE190
A	ASP194
A	ILE196
A	LEU204
A	TYR214
A	HIS225
A	TYR227
A	HOH336
A	HOH337

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE VO4 A 251

Chain	Residue
A	ARG8
A	HIS9
A	ASN15
A	ARG60
A	GLU87
A	HIS182
A	GLY183
A	3PG252
A	HOH264

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 3PG A 252

Chain	Residue
A	THR21
A	GLY22
A	GLU87
A	TYR90
A	LYS98
A	ARG114
A	ARG115
A	ASN184
A	VO4251
A	HOH254
A	HOH265
A	HOH292
A	HOH324

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PG4 B 250

Chain	Residue
A	LYS140
B	ASP51
B	ALA173
B	LYS175

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PG4 B 251

Chain	Residue
B	ILE190
B	ASP194
B	ILE196
B	TYR214
B	HIS225
B	TYR227
B	HOH332

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE VO4 B 252

Chain	Residue
B	ARG8
B	HIS9
B	ASN15
B	ARG60
B	GLU87
B	HIS182
B	GLY183
B	3PG253
B	HOH294

---

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3PG B 253

Chain	Residue
B	THR21
B	GLY22
B	GLU87
B	TYR90
B	LYS98
B	ARG114
B	ARG115
B	ASN184
B	VO4252
B	HOH280
B	HOH295

---

Functional Information from PROSITE/UniProt

site_id	PS00175
Number of Residues	10
Details	PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsTwN

Chain	Residue	Details
A	LEU6-ASN15

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:21904048

Chain	Residue	Details
A	HIS9
B	HIS9

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	GLU87
B	GLU87

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:21904048, ECO:0007744|PDB:3FDZ

Chain	Residue	Details
A	ARG8
B	ARG60
B	GLU87
B	LYS98
B	ARG114
B	GLY183
A	HIS9
A	ASN15
A	GLY22
A	TYR90
A	ARG115
A	THR21
A	HIS182
A	ASN184
B	HIS9
B	ASN15
B	GLY22
B	TYR90
B	ARG115
B	HIS182
B	ASN184
A	ARG60
A	GLU87
A	LYS98
A	ARG114
A	GLY183
B	ARG8
B	THR21

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	HIS182
B	HIS182

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
A	HIS182
A	ARG60
A	GLU87
A	HIS9

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
B	HIS182
B	ARG60
B	GLU87
B	HIS9

---