1YFK

Crystal structure of human B type phosphoglycerate mutase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004082	molecular_function	bisphosphoglycerate mutase activity
A	0004619	molecular_function	phosphoglycerate mutase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0019901	molecular_function	protein kinase binding
A	0034774	cellular_component	secretory granule lumen
A	0061621	biological_process	canonical glycolysis
A	0070062	cellular_component	extracellular exosome
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0003824	molecular_function	catalytic activity
B	0004082	molecular_function	bisphosphoglycerate mutase activity
B	0004619	molecular_function	phosphoglycerate mutase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0016853	molecular_function	isomerase activity
B	0016868	molecular_function	intramolecular phosphotransferase activity
B	0019901	molecular_function	protein kinase binding
B	0034774	cellular_component	secretory granule lumen
B	0061621	biological_process	canonical glycolysis
B	0070062	cellular_component	extracellular exosome
B	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 263

Chain	Residue
A	TRP68
A	ARG83
B	TRP68
B	ARG83

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT A 500

Chain	Residue
A	TYR92
A	LYS100
A	ARG116
A	ASN17
A	PHE22
A	SER23
A	GLY24
A	GLU89

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIT B 1500

Chain	Residue
B	ASN17
B	ARG21
B	SER23
B	GLY24
B	ARG62
B	GLU89
B	TYR92
B	LYS100
B	ARG116

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU8-ASN17

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"23653202","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15883004","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15883004","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15883004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23653202","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q3JWH7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15883004","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00950","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23653202","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DBJ1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9DBJ1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS186
A	ARG62
A	HIS11
A	GLU89

---

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

Chain	Residue	Details
B	HIS186
B	ARG62
B	HIS11
B	GLU89

---