1E58

E.coli cofactor-dependent 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	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
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	0042803	molecular_function	protein homodimerization activity
A	0061621	biological_process	canonical glycolysis
A	0097216	molecular_function	guanosine tetraphosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE SO4 A1001

Chain	Residue
A	NEP10
A	HOH2211
A	HOH2339
A	HOH2417
A	HOH2418
A	HOH2421
A	HOH2424
A	ARG20
A	PHE21
A	THR22
A	GLY23
A	ARG61
A	GLU88
A	TYR91
A	HOH2033

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A1002

Chain	Residue
A	TYR91
A	ARG115
A	ARG116
A	HOH2367
A	HOH2418
A	HOH2419
A	HOH2420
A	HOH2421
A	HOH2422

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A3001

Chain	Residue
A	TRP67
A	LYS82

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU7-ASN16

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11038361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11884145","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11038361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11884145","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11038361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11884145","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q3JWH7","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11884145","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11038361","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
A	ARG61
A	HIS183
A	GLU88

---