1IMD

STRUCTURAL STUDIES OF METAL BINDING BY INOSITOL MONOPHOSPHATASE: EVIDENCE FOR TWO-METAL ION CATALYSIS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006020	biological_process	inositol metabolic process
A	0006021	biological_process	inositol biosynthetic process
A	0006661	biological_process	phosphatidylinositol biosynthetic process
A	0006796	biological_process	phosphate-containing compound metabolic process
A	0007165	biological_process	signal transduction
A	0008934	molecular_function	inositol monophosphate 1-phosphatase activity
A	0016787	molecular_function	hydrolase activity
A	0030145	molecular_function	manganese ion binding
A	0031403	molecular_function	lithium ion binding
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0052832	molecular_function	inositol monophosphate 3-phosphatase activity
A	0052833	molecular_function	inositol monophosphate 4-phosphatase activity
A	0052834	molecular_function	inositol monophosphate phosphatase activity
B	0000287	molecular_function	magnesium ion binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006020	biological_process	inositol metabolic process
B	0006021	biological_process	inositol biosynthetic process
B	0006661	biological_process	phosphatidylinositol biosynthetic process
B	0006796	biological_process	phosphate-containing compound metabolic process
B	0007165	biological_process	signal transduction
B	0008934	molecular_function	inositol monophosphate 1-phosphatase activity
B	0016787	molecular_function	hydrolase activity
B	0030145	molecular_function	manganese ion binding
B	0031403	molecular_function	lithium ion binding
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0052832	molecular_function	inositol monophosphate 3-phosphatase activity
B	0052833	molecular_function	inositol monophosphate 4-phosphatase activity
B	0052834	molecular_function	inositol monophosphate phosphatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 278

Chain	Residue
A	GLU70
A	ASP90
A	ILE92
A	PO4280
A	HOH281

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 279

Chain	Residue
A	ASP90
A	ASP93
A	ASP220
A	PO4280

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 280

Chain	Residue
A	GLU70
A	ASP90
A	ILE92
A	ASP93
A	GLY94
A	THR95
A	MN278
A	MN279
A	HOH282
A	HOH296

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 278

Chain	Residue
B	GLU70
B	ASP90
B	ILE92
B	PO4280
B	HOH281

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 279

Chain	Residue
B	ASP90
B	ASP93
B	ASP220
B	PO4280

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 280

Chain	Residue
B	GLU70
B	ASP90
B	ILE92
B	ASP93
B	GLY94
B	THR95
B	MN278
B	MN279
B	HOH282

---

site_id	M1
Number of Residues	8
Details

Chain	Residue
A	GLU70
A	ASP90
A	PRO91
A	ILE92
A	ASP93
A	GLY94
A	THR95
A	ASP220

---

site_id	M2
Number of Residues	8
Details

Chain	Residue
B	ASP90
B	PRO91
B	ILE92
B	ASP93
B	GLY94
B	THR95
B	ASP220
B	GLU70

---

Functional Information from PROSITE/UniProt

site_id	PS00629
Number of Residues	14
Details	IMP_1 Inositol monophosphatase family signature 1. WiIDPIDGTtnFvH

Chain	Residue	Details
A	TRP87-HIS100

---

site_id	PS00630
Number of Residues	15
Details	IMP_2 Inositol monophosphatase family signature 2. WDvAGAgIIVteaGG

Chain	Residue	Details
A	TRP219-GLY233

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:8068620, ECO:0000303|PubMed:8068621

Chain	Residue	Details
A	GLU70
A	GLU213
B	GLU70
B	GLU213

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:23027737, ECO:0000269|PubMed:8068621

Chain	Residue	Details
A	ASP90
A	ASP93
B	ASP90
B	ASP93

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:23027737, ECO:0000269|PubMed:8068621, ECO:0000303|PubMed:1332026, ECO:0000303|PubMed:8068620

Chain	Residue	Details
A	ILE92
B	ILE92

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:8068620

Chain	Residue	Details
A	GLY194
A	ASP220
B	GLY194
B	ASP220

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR168
B	THR168

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 577

Chain	Residue	Details
A	GLU70	metal ligand, proton acceptor, proton donor
A	ASP90	metal ligand
A	ILE92	metal ligand
A	ASP93	metal ligand
A	THR95	hydrogen bond acceptor
A	ASP220	metal ligand

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 577

Chain	Residue	Details
B	GLU70	metal ligand, proton acceptor, proton donor
B	ASP90	metal ligand
B	ILE92	metal ligand
B	ASP93	metal ligand
B	THR95	hydrogen bond acceptor
B	ASP220	metal ligand

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