3HSK

Crystal Structure of Aspartate Semialdehyde Dehydrogenase with NADP from Candida albicans

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004073	molecular_function	aspartate-semialdehyde dehydrogenase activity
A	0005575	cellular_component	cellular_component
A	0005634	cellular_component	nucleus
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009086	biological_process	methionine biosynthetic process
A	0009088	biological_process	threonine biosynthetic process
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
A	0009090	biological_process	homoserine biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
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	0000166	molecular_function	nucleotide binding
B	0004073	molecular_function	aspartate-semialdehyde dehydrogenase activity
B	0005575	cellular_component	cellular_component
B	0005634	cellular_component	nucleus
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0009086	biological_process	methionine biosynthetic process
B	0009088	biological_process	threonine biosynthetic process
B	0009089	biological_process	lysine biosynthetic process via diaminopimelate
B	0009090	biological_process	homoserine biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
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	12
Details	BINDING SITE FOR RESIDUE NAP A 366

Chain	Residue
A	GLY10
A	ASP86
A	VAL89
A	GLY194
A	THR12
A	GLY13
A	SER14
A	ALA36
A	SER37
A	SER40
A	GLY84
A	LEU85

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL243-THR257

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PIRSR","id":"PIRSR000148-1","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PIRSR","id":"PIRSR000148-1","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24025428","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HSK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A179UL48","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A080WMA9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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