Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2QZ9

crystal structure of aspartate semialdehyde dehydrogenase II from vibrio cholerae

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	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
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	0009085	biological_process	lysine 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	0009097	biological_process	isoleucine 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	0019877	biological_process	diaminopimelate biosynthetic process
B	0046983	molecular_function	protein dimerization activity
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
B	0071266	biological_process	'de novo' L-methionine biosynthetic process
C	0004073	molecular_function	aspartate-semialdehyde dehydrogenase activity
C	0006520	biological_process	amino acid metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0009085	biological_process	lysine biosynthetic process
C	0009086	biological_process	methionine biosynthetic process
C	0009088	biological_process	threonine biosynthetic process
C	0009089	biological_process	lysine biosynthetic process via diaminopimelate
C	0009097	biological_process	isoleucine biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0019877	biological_process	diaminopimelate biosynthetic process
C	0046983	molecular_function	protein dimerization activity
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
C	0071266	biological_process	'de novo' L-methionine biosynthetic process

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL233-ALA247

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Acyl-thioester intermediate => ECO:0000269\|PubMed:18323627

Chain	Residue	Details
A	CYS133
B	CYS133
C	CYS133

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_02121

Chain	Residue	Details
A	HIS246
B	HIS246
C	HIS246

site_id	SWS_FT_FI3
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_02121

Chain	Residue	Details
A	THR14
B	ARG42
B	ARG102
B	GLN160
B	SER163
B	LYS217
B	ARG239
B	ASN317
C	THR14
C	ARG42
C	ARG102
A	ARG42
C	GLN160
C	SER163
C	LYS217
C	ARG239
C	ASN317
A	ARG102
A	GLN160
A	SER163
A	LYS217
A	ARG239
A	ASN317
B	THR14

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1brm

Chain	Residue	Details
A	CYS133
A	HIS246
A	GLN160

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1brm

Chain	Residue	Details
B	CYS133
B	HIS246
B	GLN160

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1brm

Chain	Residue	Details
C	CYS133
C	HIS246
C	GLN160

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1brm

Chain	Residue	Details
A	CYS133
A	GLN160

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1brm

Chain	Residue	Details
B	CYS133
B	GLN160

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1brm

Chain	Residue	Details
C	CYS133
C	GLN160

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)