1PS8

Crystal Structure of the R270K Mutant of Aspartate Semialdehyde dehydrogenase from Haemophilus influenzae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004073	molecular_function	aspartate-semialdehyde dehydrogenase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009085	biological_process	lysine 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	0009097	biological_process	isoleucine 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	0019877	biological_process	diaminopimelate biosynthetic process
A	0046983	molecular_function	protein dimerization activity
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
A	0071266	biological_process	'de novo' L-methionine biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Acyl-thioester intermediate => ECO:0000269|PubMed:14559965, ECO:0000269|PubMed:15272161

Chain	Residue	Details
A	CYS136

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:14559965

Chain	Residue	Details
A	HIS277

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site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:15272161

Chain	Residue	Details
A	THR37
A	GLN74
A	SER166
A	GLN353
A	ARG10

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:14559965

Chain	Residue	Details
A	ARG103
A	LYS246

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site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:15272161

Chain	Residue	Details
A	LYS270
A	GLN163
A	GLU243

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