9IX7

Crystal structure of homolog of dihydroxyacid dehydratase(AstD) from Aspergillus terreus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004160	molecular_function	dihydroxy-acid dehydratase activity
A	0005739	cellular_component	mitochondrion
A	0008652	biological_process	amino acid biosynthetic process
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0009097	biological_process	isoleucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0004160	molecular_function	dihydroxy-acid dehydratase activity
B	0005739	cellular_component	mitochondrion
B	0008652	biological_process	amino acid biosynthetic process
B	0009082	biological_process	branched-chain amino acid biosynthetic process
B	0009097	biological_process	isoleucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PROSITE/UniProt

site_id	PS00886
Number of Residues	11
Details	ILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKnmPGvlmA

Chain	Residue	Details
A	CYS159-ALA169

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site_id	PS00887
Number of Residues	12
Details	ILVD_EDD_2 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 2. ALLTDGRFSGGS

Chain	Residue	Details
A	ALA503-SER514

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