7KIO

Crystal structure of inositol polyphosphate 1-phosphatase (INPP1) D54A mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004441	molecular_function	inositol-1,4-bisphosphate 1-phosphatase activity
A	0016787	molecular_function	hydrolase activity
A	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0052829	molecular_function	inositol-1,3,4-trisphosphate 1-phosphatase activity

Functional Information from PROSITE/UniProt

site_id	PS00629
Number of Residues	13
Details	IMP_1 Inositol monophosphatase family signature 1. W.VDPIDSTyqYiK

Chain	Residue	Details
A	TRP151-LYS163

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

Chain	Residue	Details
A	TRP316-GLY330

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:33172890

Chain	Residue	Details
A	GLU80
A	ALA54

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:7947723, ECO:0000312|PDB:1INP

Chain	Residue	Details
A	ASP153
A	ILE155
A	ASP317
A	GLU79

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site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:33172890, ECO:0007744|PDB:7KIR

Chain	Residue	Details
A	THR158
A	SER268
A	LYS270
A	GLY290
A	ALA291
A	LYS294
A	THR312
A	SER157
A	ASP156

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49441

Chain	Residue	Details
A	SER318

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 856

Chain	Residue	Details
A	ALA54	electrostatic stabiliser, proton acceptor, proton donor
A	GLU79	metal ligand
A	ASP153	metal ligand
A	ILE155	metal ligand
A	ASP156	metal ligand
A	THR158	electrostatic stabiliser, enhance reactivity, increase nucleophilicity, proton acceptor, proton donor, proton relay
A	ASP317	metal ligand

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