1HOX

CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE COMPLEXED WITH FRUCTOSE-6-PHOSPHATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004347	molecular_function	glucose-6-phosphate isomerase activity
A	0005125	molecular_function	cytokine activity
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0007165	biological_process	signal transduction
A	0016853	molecular_function	isomerase activity
A	0048029	molecular_function	monosaccharide binding
A	0051156	biological_process	glucose 6-phosphate metabolic process
A	0097367	molecular_function	carbohydrate derivative binding
A	1901135	biological_process	carbohydrate derivative metabolic process
B	0004347	molecular_function	glucose-6-phosphate isomerase activity
B	0005125	molecular_function	cytokine activity
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0007165	biological_process	signal transduction
B	0016853	molecular_function	isomerase activity
B	0048029	molecular_function	monosaccharide binding
B	0051156	biological_process	glucose 6-phosphate metabolic process
B	0097367	molecular_function	carbohydrate derivative binding
B	1901135	biological_process	carbohydrate derivative metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00174
Number of Residues	18
Details	P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GvVWdinsFDQwGVElgK

Chain	Residue	Details
A	GLY501-LYS518

---

site_id	PS00765
Number of Residues	14
Details	P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG

Chain	Residue	Details
A	ASP267-GLY280

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11327814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11425306","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"11327814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11425306","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11425306","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HOX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P06745","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q6P6V0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06745","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	7
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
A	HIS388
B	ARG272
B	LYS518
B	GLU216
B	GLU357
B	LYS210
B	GLY271

---

site_id	CSA2
Number of Residues	7
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
A	ARG272
A	LYS518
A	GLU216
A	GLU357
A	LYS210
A	GLY271
B	HIS388

---

site_id	MCSA1
Number of Residues	7
Details	M-CSA 842

Chain	Residue	Details
A	LYS210	electrostatic stabiliser
A	GLU216	modifies pKa
A	GLY271	electrostatic stabiliser
A	ARG272	electrostatic stabiliser
A	GLU357	proton acceptor, proton donor
A	HIS388	proton acceptor, proton donor
A	LYS518	proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 842

Chain	Residue	Details
B	LYS210	electrostatic stabiliser
B	GLU216	modifies pKa
B	GLY271	electrostatic stabiliser
B	ARG272	electrostatic stabiliser
B	GLU357	proton acceptor, proton donor
B	HIS388	proton acceptor, proton donor
B	LYS518	proton acceptor, proton donor

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