6C85

Crystal structure of aspartate semialdehyde dehydrogenase from Blastomyces dermatitidis with p-benzoquinone

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004073	molecular_function	aspartate-semialdehyde dehydrogenase activity
A	0006520	biological_process	amino acid metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0046983	molecular_function	protein dimerization activity
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0004073	molecular_function	aspartate-semialdehyde dehydrogenase activity
B	0006520	biological_process	amino acid metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0046983	molecular_function	protein dimerization activity
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue PLQ A 401

Chain	Residue
A	ARG114
A	ASN153
A	CYS154
A	GLY186
A	LYS211

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site_id	AC2
Number of Residues	6
Details	binding site for residue PLQ B 401

Chain	Residue
B	LYS211
B	HOH531
B	ARG114
B	ASN153
B	CYS154
B	GLY186

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Functional Information from PROSITE/UniProt

site_id	PS01103
Number of Residues	15
Details	ASD Aspartate-semialdehyde dehydrogenase signature. VSvaCnRVpvldGHT

Chain	Residue	Details
A	VAL238-THR252

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