Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5BNT

X-ray Crystal Structure of a Aspartate-semialdehyde dehydrogenase bound to NADP from Pseudomonas aeruginosa

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue NAP C 500

Chain	Residue
C	GLY8
C	GLY74
C	HOH605
C	HOH626
C	HOH630
C	HOH649
C	HOH652
C	HOH667
C	HOH690
C	HOH719
C	HOH785
C	ARG10
C	GLY11
C	MET12
C	VAL13
C	THR37
C	SER38
C	CYS72
C	GLN73

site_id	AC2
Number of Residues	11
Details	binding site for residue NAP B 500

Chain	Residue
B	GLY8
B	ARG10
B	GLY11
B	MET12
B	VAL13
B	THR36
B	THR37
B	SER38
B	GLN73
B	HOH610
B	HOH677

site_id	AC3
Number of Residues	30
Details	binding site for residue NAP A 500

Chain	Residue
A	GLY8
A	ARG10
A	GLY11
A	MET12
A	VAL13
A	THR36
A	THR37
A	SER38
A	CYS72
A	GLN73
A	GLY74
A	ALA97
A	SER165
A	GLY166
A	GLY168
A	ALA169
A	GLN351
A	LEU352
A	GLY355
A	ALA356
A	HOH612
A	HOH613
A	HOH631
A	HOH646
A	HOH674
A	HOH700
A	HOH702
A	HOH721
A	HOH722
A	HOH739

site_id	AC4
Number of Residues	21
Details	binding site for residue NAP D 500

Chain	Residue
D	GLY8
D	ARG10
D	GLY11
D	MET12
D	VAL13
D	THR36
D	THR37
D	SER38
D	CYS72
D	GLN73
D	GLY74
D	HOH603
D	HOH604
D	HOH633
D	HOH665
D	HOH673
D	HOH689
D	HOH694
D	HOH705
D	HOH749
D	HOH753

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	VAL262-SER276

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Acyl-thioester intermediate => ECO:0000250

Chain	Residue	Details
C	CYS135
B	CYS135
A	CYS135
D	CYS135

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250

Chain	Residue	Details
C	HIS275
B	HIS275
A	HIS275
D	HIS275

site_id	SWS_FT_FI3
Number of Residues	44
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
C	GLN162
C	SER165
C	PRO193
C	GLU241
C	LYS244
C	ARG268
C	GLN351
B	ARG10
B	THR37
B	GLN73
B	ARG102
B	GLN162
B	SER165
B	PRO193
B	GLU241
B	LYS244
B	ARG268
B	GLN351
A	ARG10
A	THR37
A	GLN73
A	ARG102
A	GLN162
A	SER165
A	PRO193
A	GLU241
A	LYS244
A	ARG268
A	GLN351
D	ARG10
D	THR37
D	GLN73
D	ARG102
D	GLN162
D	SER165
D	PRO193
D	GLU241
D	LYS244
D	ARG268
D	GLN351
C	ARG10
C	THR37
C	GLN73
C	ARG102

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