Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5PGM

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

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	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	0016853	molecular_function	isomerase activity
B	0016868	molecular_function	intramolecular phosphotransferase activity
B	0061621	biological_process	canonical glycolysis
C	0003824	molecular_function	catalytic activity
C	0004619	molecular_function	phosphoglycerate mutase activity
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005741	cellular_component	mitochondrial outer membrane
C	0005758	cellular_component	mitochondrial intermembrane space
C	0005829	cellular_component	cytosol
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0016853	molecular_function	isomerase activity
C	0016868	molecular_function	intramolecular phosphotransferase activity
C	0061621	biological_process	canonical glycolysis
D	0003824	molecular_function	catalytic activity
D	0004619	molecular_function	phosphoglycerate mutase activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005741	cellular_component	mitochondrial outer membrane
D	0005758	cellular_component	mitochondrial intermembrane space
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0016853	molecular_function	isomerase activity
D	0016868	molecular_function	intramolecular phosphotransferase activity
D	0061621	biological_process	canonical glycolysis
E	0003824	molecular_function	catalytic activity
E	0004619	molecular_function	phosphoglycerate mutase activity
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005741	cellular_component	mitochondrial outer membrane
E	0005758	cellular_component	mitochondrial intermembrane space
E	0005829	cellular_component	cytosol
E	0006094	biological_process	gluconeogenesis
E	0006096	biological_process	glycolytic process
E	0016853	molecular_function	isomerase activity
E	0016868	molecular_function	intramolecular phosphotransferase activity
E	0061621	biological_process	canonical glycolysis
F	0003824	molecular_function	catalytic activity
F	0004619	molecular_function	phosphoglycerate mutase activity
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005741	cellular_component	mitochondrial outer membrane
F	0005758	cellular_component	mitochondrial intermembrane space
F	0005829	cellular_component	cytosol
F	0006094	biological_process	gluconeogenesis
F	0006096	biological_process	glycolytic process
F	0016853	molecular_function	isomerase activity
F	0016868	molecular_function	intramolecular phosphotransferase activity
F	0061621	biological_process	canonical glycolysis
G	0003824	molecular_function	catalytic activity
G	0004619	molecular_function	phosphoglycerate mutase activity
G	0005737	cellular_component	cytoplasm
G	0005739	cellular_component	mitochondrion
G	0005741	cellular_component	mitochondrial outer membrane
G	0005758	cellular_component	mitochondrial intermembrane space
G	0005829	cellular_component	cytosol
G	0006094	biological_process	gluconeogenesis
G	0006096	biological_process	glycolytic process
G	0016853	molecular_function	isomerase activity
G	0016868	molecular_function	intramolecular phosphotransferase activity
G	0061621	biological_process	canonical glycolysis
H	0003824	molecular_function	catalytic activity
H	0004619	molecular_function	phosphoglycerate mutase activity
H	0005737	cellular_component	cytoplasm
H	0005739	cellular_component	mitochondrion
H	0005741	cellular_component	mitochondrial outer membrane
H	0005758	cellular_component	mitochondrial intermembrane space
H	0005829	cellular_component	cytosol
H	0006094	biological_process	gluconeogenesis
H	0006096	biological_process	glycolytic process
H	0016853	molecular_function	isomerase activity
H	0016868	molecular_function	intramolecular phosphotransferase activity
H	0061621	biological_process	canonical glycolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 D 300

Chain	Residue
D	HIS8
D	SER11
D	ASN14
D	THR20
D	ARG59
D	HOH428
D	HOH431
D	HOH508
D	HOH549

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 301

Chain	Residue
D	ARG87
D	TYR89
D	ARG113
D	ARG114
D	HOH490
D	HOH588

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 C 300

Chain	Residue
C	HIS8
C	SER11
C	ASN14
C	THR20
C	ARG59
C	HOH555
C	HOH597
C	HOH657
C	HOH662

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 301

Chain	Residue
C	TYR89
C	LYS97
C	ARG113
C	ARG114
C	HOH616

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 300

Chain	Residue
A	SER11
A	ASN14
A	THR20
A	ARG59
A	HOH430
A	HOH433
A	HOH512
A	HOH555
A	HOH563

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 301

Chain	Residue
A	ARG87
A	TYR89
A	ARG113
A	ARG114
A	ASN183
A	HOH493
A	HOH506
A	HOH553
A	HOH603

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 300

Chain	Residue
B	HIS8
B	SER11
B	ASN14
B	THR20
B	ARG59
B	HOH432
B	HOH476
B	HOH515
B	HOH578

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 301

Chain	Residue
B	PHE19
B	TYR89
B	LYS97
B	ARG113
B	HOH495

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 E 300

Chain	Residue
E	HOH431
E	HOH508
E	HOH549
E	HIS8
E	SER11
E	ASN14
E	THR20
E	ARG59
E	HOH428

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 301

Chain	Residue
E	ARG87
E	TYR89
E	ARG113
E	ARG114
E	HOH490
E	HOH588

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 F 300

Chain	Residue
F	HIS8
F	SER11
F	ASN14
F	THR20
F	ARG59
F	HOH555
F	HOH597
F	HOH657
F	HOH662

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 301

Chain	Residue
F	TYR89
F	LYS97
F	ARG113
F	ARG114
F	HOH616

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 G 300

Chain	Residue
G	SER11
G	ASN14
G	THR20
G	ARG59
G	HOH594
G	HOH597
G	HOH676
G	HOH719
G	HOH727

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 G 301

Chain	Residue
G	ARG87
G	TYR89
G	ARG113
G	ARG114
G	ASN183
G	HOH657
G	HOH670
G	HOH717
G	HOH766

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 H 300

Chain	Residue
H	HIS8
H	SER11
H	ASN14
H	THR20
H	ARG59
H	HOH432
H	HOH476
H	HOH515
H	HOH578

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 H 301

Chain	Residue
H	PHE19
H	TYR89
H	LYS97
H	ARG113
H	HOH495

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ALA E 302

Chain	Residue
E	GLU231
E	ALA233
E	ALA234

site_id	CIA
Number of Residues	4
Details	CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME.

Chain	Residue
A	HIS8
A	HIS181
A	ARG7
A	ARG59

site_id	CIB
Number of Residues	4
Details	CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME.

Chain	Residue
B	HIS8
B	HIS181
B	ARG7
B	ARG59

site_id	CIC
Number of Residues	4
Details	CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME.

Chain	Residue
C	HIS181
C	ARG7
C	ARG59
C	HIS8

site_id	CID
Number of Residues	4
Details	CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME.

Chain	Residue
D	HIS8
D	HIS181
D	ARG7
D	ARG59

site_id	CIE
Number of Residues	4
Details	CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME.

Chain	Residue
E	HIS8
E	HIS181
E	ARG7
E	ARG59

site_id	CIF
Number of Residues	4
Details	CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME.

Chain	Residue
F	HIS8
F	HIS181
F	ARG7
F	ARG59

site_id	CIG
Number of Residues	4
Details	CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME.

Chain	Residue
G	HIS8
G	HIS181
G	ARG7
G	ARG59

site_id	CIH
Number of Residues	4
Details	CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME.

Chain	Residue
H	HIS8
H	HIS181
H	ARG7
H	ARG59

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	LEU5-ASN14

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"10064712","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115412","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9512715","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10064712","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10369755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115412","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10369755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531478","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10531478","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10369755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115412","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10369755","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"10064712","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	16
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	56
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

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	HIS181	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	HIS181	electrostatic stabiliser

site_id	MCSA3
Number of Residues	4
Details	M-CSA 504

Chain	Residue	Details
C	HIS8	covalent catalysis
C	ARG59	electrostatic stabiliser
C	GLU86	proton donor, proton shuttle (general acid/base)
C	HIS181	electrostatic stabiliser

site_id	MCSA4
Number of Residues	4
Details	M-CSA 504

Chain	Residue	Details
D	HIS8	covalent catalysis
D	ARG59	electrostatic stabiliser
D	GLU86	proton donor, proton shuttle (general acid/base)
D	HIS181	electrostatic stabiliser

site_id	MCSA5
Number of Residues	4
Details	M-CSA 504

Chain	Residue	Details
E	HIS8	covalent catalysis
E	ARG59	electrostatic stabiliser
E	GLU86	proton donor, proton shuttle (general acid/base)
E	HIS181	electrostatic stabiliser

site_id	MCSA6
Number of Residues	4
Details	M-CSA 504

Chain	Residue	Details
F	HIS8	covalent catalysis
F	ARG59	electrostatic stabiliser
F	GLU86	proton donor, proton shuttle (general acid/base)
F	HIS181	electrostatic stabiliser

site_id	MCSA7
Number of Residues	4
Details	M-CSA 504

Chain	Residue	Details
G	HIS8	covalent catalysis
G	ARG59	electrostatic stabiliser
G	GLU86	proton donor, proton shuttle (general acid/base)
G	HIS181	electrostatic stabiliser

site_id	MCSA8
Number of Residues	4
Details	M-CSA 504

Chain	Residue	Details
H	HIS8	covalent catalysis
H	ARG59	electrostatic stabiliser
H	GLU86	proton donor, proton shuttle (general acid/base)
H	HIS181	electrostatic stabiliser

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

Chain	Residue	Details
D	HIS181
D	HIS8
D	GLU86
D	ARG59

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

Chain	Residue	Details
C	HIS181
C	HIS8
C	GLU86
C	ARG59

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
A	HIS181
A	HIS8
A	GLU86
A	ARG59

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
B	HIS181
B	HIS8
B	GLU86
B	ARG59

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
E	HIS181
E	HIS8
E	GLU86
E	ARG59

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
F	HIS181
F	HIS8
F	GLU86
F	ARG59

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
G	HIS181
G	HIS8
G	GLU86
G	ARG59

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
H	HIS181
H	HIS8
H	GLU86
H	ARG59

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)