2A0N

Crystal structure of Imidazole glycerol phosphate synthase subunit hisF (EC 4.1.3.-) (tm1036) from Thermotoga maritima at 1.64 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0000107	molecular_function	imidazoleglycerol-phosphate synthase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0008652	biological_process	amino acid biosynthetic process
A	0016829	molecular_function	lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 254

Chain	Residue
A	SER101
A	PO4261

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 255

Chain	Residue
A	ARG163

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 257

Chain	Residue
A	GLU251
A	HOH577

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site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 258

Chain	Residue
A	GLU34
A	GLN72

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site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD A 259

Chain	Residue
A	HOH458
A	HOH377
A	HOH412

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site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 261

Chain	Residue
A	GLY82
A	ASN103
A	THR104
A	IOD254
A	HOH302
A	HOH401
A	HOH533
A	HOH535

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site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE UNL A 300

Chain	Residue
A	CYS9
A	ASP11
A	ASP176
A	GLY177
A	LEU222
A	ALA223
A	ALA224
A	SER225
A	VAL226
A	HOH306
A	HOH489
A	HOH518
A	HOH530
A	HOH531
A	HOH532
A	HOH538
A	HOH542
A	HOH569

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 753

Chain	Residue	Details
A	ASP11	proton acceptor, proton donor
A	ASP130	proton acceptor, proton donor

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site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 11264293

Chain	Residue	Details
A	ASP11

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