Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6GJ0

Human IMPase with Mn

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004346	molecular_function	glucose-6-phosphatase activity
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	0008877	molecular_function	glucose-1-phosphatase activity
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	0047954	molecular_function	glycerol-2-phosphatase activity
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
A	0103026	molecular_function	fructose-1-phosphatase activity
B	0000287	molecular_function	magnesium ion binding
B	0004346	molecular_function	glucose-6-phosphatase activity
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	0008877	molecular_function	glucose-1-phosphatase activity
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	0047954	molecular_function	glycerol-2-phosphatase activity
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
B	0103026	molecular_function	fructose-1-phosphatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MN A 301

Chain	Residue
A	GLU70
A	MES307
A	HOH429
A	HOH432
A	HOH456

site_id	AC2
Number of Residues	5
Details	binding site for residue MN A 302

Chain	Residue
A	HOH492
A	GLU70
A	ASP90
A	ILE92
A	MES307

site_id	AC3
Number of Residues	6
Details	binding site for residue MN A 303

Chain	Residue
A	ASP90
A	ASP93
A	ASP220
A	GOL304
A	MES307
A	HOH528

site_id	AC4
Number of Residues	10
Details	binding site for residue GOL A 304

Chain	Residue
A	ASP93
A	THR195
A	ALA196
A	GLU213
A	ASP220
A	MN303
A	MES307
A	HOH446
A	HOH528
A	HOH552

site_id	AC5
Number of Residues	7
Details	binding site for residue GOL A 305

Chain	Residue
A	LEU163
A	SER192
A	HOH407
A	HOH411
B	ILE190
B	ARG191
B	SER192

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL A 306

Chain	Residue
A	ARG248
A	LEU271
A	GLN272
A	HOH557

site_id	AC7
Number of Residues	16
Details	binding site for residue MES A 307

Chain	Residue
A	GLU70
A	ASP90
A	ILE92
A	ASP93
A	GLY94
A	THR95
A	THR96
A	MN301
A	MN302
A	MN303
A	GOL304
A	HOH426
A	HOH489
A	HOH528
A	HOH574
A	HOH585

site_id	AC8
Number of Residues	6
Details	binding site for residue MN B 301

Chain	Residue
B	ASP90
B	ASP93
B	ASP220
B	GOL304
B	MES307
B	HOH517

site_id	AC9
Number of Residues	5
Details	binding site for residue MN B 302

Chain	Residue
B	GLU70
B	ASP90
B	ILE92
B	MES307
B	HOH472

site_id	AD1
Number of Residues	5
Details	binding site for residue MN B 303

Chain	Residue
B	GLU70
B	MES307
B	HOH428
B	HOH436
B	HOH447

site_id	AD2
Number of Residues	11
Details	binding site for residue GOL B 304

Chain	Residue
B	ASP93
B	THR195
B	ALA196
B	GLU213
B	ASP220
B	MN301
B	MES307
B	HOH413
B	HOH441
B	HOH517
B	HOH540

site_id	AD3
Number of Residues	8
Details	binding site for residue GOL B 305

Chain	Residue
A	VAL99
A	HIS100
B	GLN151
B	LYS156
B	HIS188
B	ASP209
B	HOH534
B	HOH539

site_id	AD4
Number of Residues	4
Details	binding site for residue GOL B 306

Chain	Residue
B	VAL73
B	LYS78
B	SER79
B	ASP277

site_id	AD5
Number of Residues	19
Details	binding site for residue MES B 307

Chain	Residue
B	THR95
B	THR96
B	ASN97
B	GLY194
B	MN301
B	MN302
B	MN303
B	GOL304
B	HOH428
B	HOH429
B	HOH496
B	HOH517
A	ARG191
A	HOH536
B	GLU70
B	ASP90
B	ILE92
B	ASP93
B	GLY94

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	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8068620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8068621","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23027737","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8068621","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23027737","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8068621","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1332026","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"8068620","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8068620","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)