3PGM

THE STRUCTURE OF YEAST PHOSPHOGLYCERATE MUTASE AT 0.28 NM RESOLUTION

Replaces:  1PGM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004619	molecular_function	phosphoglycerate mutase activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005741	cellular_component	mitochondrial outer membrane
A	0005758	cellular_component	mitochondrial intermembrane space
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016020	cellular_component	membrane
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0061621	biological_process	canonical glycolysis
B	0003824	molecular_function	catalytic activity
B	0004619	molecular_function	phosphoglycerate mutase activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005741	cellular_component	mitochondrial outer membrane
B	0005758	cellular_component	mitochondrial intermembrane space
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016020	cellular_component	membrane
B	0016853	molecular_function	isomerase activity
B	0016868	molecular_function	intramolecular phosphotransferase activity
B	0061621	biological_process	canonical glycolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 245

Chain	Residue
A	HIS8
A	GLU86
A	HIS179
A	3PG247

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 245

Chain	Residue
B	HIS8
B	GLU86
B	HIS179
B	3PG247

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 246

Chain	Residue
A	GLN10
A	SER11
A	ASN14
A	GLU15
A	THR20
A	3PG247
A	HIS8

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 3PG A 247

Chain	Residue
A	HIS8
A	SER11
A	GLU15
A	THR20
A	GLU86
A	HIS179
A	SO4245
A	SO4246

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 246

Chain	Residue
B	HIS8
B	GLN10
B	SER11
B	ASN14
B	GLU15
B	THR20
B	3PG247

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 3PG B 247

Chain	Residue
B	HIS8
B	SER11
B	GLU15
B	THR20
B	GLU86
B	HIS179
B	SO4245
B	SO4246

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU5-ASN14

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:10064712, ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412, ECO:0000269|PubMed:9512715

Chain	Residue	Details
A	GLY9
B	GLY9

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10064712

Chain	Residue	Details
A	ARG87
B	ARG87

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412

Chain	Residue	Details
A	HIS8
B	HIS8

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478

Chain	Residue	Details
A	GLY21
B	GLY21

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10531478

Chain	Residue	Details
A	ALA60
B	ALA60

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:6115412

Chain	Residue	Details
A	ARG87
A	LEU183
B	ARG87
B	LEU183

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10369755

Chain	Residue	Details
A	ALA98
A	ARG114
B	ALA98
B	ARG114

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000305|PubMed:10064712

Chain	Residue	Details
A	SER182
B	SER182

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358

Chain	Residue	Details
A	GLU12
A	GLY185
B	GLU12
B	GLY185

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	VAL49
B	VAL49

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	PHE116
B	PHE116

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956

Chain	Residue	Details
A	SER127
B	SER127

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	PRO128
B	PRO128

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	ASP197
B	ASP197

---

site_id	SWS_FT_FI15
Number of Residues	14
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047

Chain	Residue	Details
A	GLY31
B	LEU57
B	ALA71
B	TYR139
B	MET175
B	GLU191
A	LEU57
A	ALA71
A	TYR139
A	MET175
A	GLU191
B	GLY31

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS179
A	HIS8
A	GLU86
A	ARG59

---

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

Chain	Residue	Details
B	HIS179
B	HIS8
B	GLU86
B	ARG59

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 504

Chain	Residue	Details
A	HIS8	covalent catalysis
A	ARG59	electrostatic stabiliser
A	GLU86	proton donor, proton shuttle (general acid/base)
A	HIS179	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 504

Chain	Residue	Details
B	HIS8	covalent catalysis
B	ARG59	electrostatic stabiliser
B	GLU86	proton donor, proton shuttle (general acid/base)
B	HIS179	electrostatic stabiliser

---