1DKQ

CRYSTAL STRUCTURE OF PHYTATE COMPLEX ESCHERICHIA COLI PHYTASE AT PH 5.0. PHYTATE IS BOUND WITH ITS 3-PHOSPHATE IN THE ACTIVE SITE. HG2+ CATION ACTS AS AN INTERMOLECULAR BRIDGE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003924	molecular_function	GTPase activity
A	0003993	molecular_function	acid phosphatase activity
A	0008252	molecular_function	nucleotidase activity
A	0008707	molecular_function	4-phytase activity
A	0016036	biological_process	cellular response to phosphate starvation
A	0016787	molecular_function	hydrolase activity
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0050308	molecular_function	sugar-phosphatase activity
A	0052745	molecular_function	inositol phosphate phosphatase activity
A	0071454	biological_process	cellular response to anoxia

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE HG A 500

Chain	Residue
A	HIS113
A	ASP154
A	HIS158
A	TYR289
A	HOH674

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE HG A 501

Chain	Residue
A	HOH769
A	HIS282
A	GLN285
A	GLN287
A	LEU293

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE HG A 502

Chain	Residue
A	ARG16
A	GLU219
A	HIS250
A	ASP304
A	ASP325
A	THR327
A	HG503
A	IHP550

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE HG A 503

Chain	Residue
A	HIS250
A	ASP304
A	ASP325
A	THR327
A	HG502

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site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE IHP A 550

Chain	Residue
A	ARG16
A	ARG20
A	THR23
A	LYS24
A	ASP90
A	ARG92
A	MET216
A	GLU219
A	HIS250
A	PHE254
A	ARG267
A	HIS303
A	ASP304
A	THR305
A	HG502
A	HOH614
A	HOH639
A	HOH689
A	HOH696
A	HOH789

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Functional Information from PROSITE/UniProt

site_id	PS00778
Number of Residues	17
Details	HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. VlFIaGHDTNLanLggA

Chain	Residue	Details
A	VAL297-ALA313

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:10655611, ECO:0000305|PubMed:1429631

Chain	Residue	Details
A	ALA17

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:10655611, ECO:0000305|PubMed:8407904

Chain	Residue	Details
A	ASP304

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ

Chain	Residue	Details
A	ARG16
A	ARG20
A	ARG92
A	HIS303

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:10655611, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ

Chain	Residue	Details
A	ARG267

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