1GZV

The crystal structure of phosphoglucose isomerase from pig muscle complexed with 5-phosphoarabinonate

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PA5 A 600

Chain	Residue
A	ILE156
A	GLU357
A	HIS388
A	LYS518
A	GLY157
A	GLY158
A	SER159
A	SER209
A	LYS210
A	THR211
A	THR214
A	GLN353

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Functional Information from PROSITE/UniProt

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

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	1
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P06745

Chain	Residue	Details
A	SER358

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P06745

Chain	Residue	Details
A	ALA389
A	GLN519

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P06745

Chain	Residue	Details
A	SER159
A	LYS210
A	GLY354
A	SER358
A	ALA389
A	GLN519

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	ALA2

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	LEU12
A	GLY142

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	ASP34

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	ASN107
A	PRO455

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	PRO109

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	ASN185

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0

Chain	Residue	Details
A	THR250

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06745

Chain	Residue	Details
A	SER454

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