Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4I3V

Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetaldehyde and cofactor NAD+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
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
B	0000166	molecular_function	nucleotide binding
B	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
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
C	0000166	molecular_function	nucleotide binding
C	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
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
D	0000166	molecular_function	nucleotide binding
D	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
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
E	0000166	molecular_function	nucleotide binding
E	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
E	0016491	molecular_function	oxidoreductase activity
E	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F	0000166	molecular_function	nucleotide binding
F	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
F	0016491	molecular_function	oxidoreductase activity
F	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
G	0000166	molecular_function	nucleotide binding
G	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
G	0016491	molecular_function	oxidoreductase activity
G	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
H	0000166	molecular_function	nucleotide binding
H	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
H	0016491	molecular_function	oxidoreductase activity
H	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NAD A 501

Chain	Residue
A	ILE154
A	PHE232
A	SER235
A	VAL238
A	LEU241
A	HOH737
A	HOH765
A	HOH771
A	HOH930
A	THR155
A	PRO156
A	PHE157
A	LYS181
A	THR183
A	GLU184
A	PRO214
A	GLY218

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE POA A 502

Chain	Residue
A	ARG108
A	ASN158
A	HIS159
A	MET163
A	GLU254
A	ARG290
A	CYS291
A	THR292
A	ARG447
A	HOH618
A	HOH647

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NAD B 501

Chain	Residue
B	ILE154
B	THR155
B	PRO156
B	PHE157
B	LYS181
B	THR183
B	GLU184
B	PRO214
B	GLY218
B	PHE232
B	SER235
B	VAL238
B	LEU241
B	HOH641
B	HOH745
B	HOH831

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POA B 502

Chain	Residue
B	ARG108
B	HIS159
B	GLU254
B	ARG290
B	CYS291
B	THR292
B	ARG447
B	HOH604
B	HOH683
B	HOH972

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NAD C 501

Chain	Residue
C	ILE154
C	THR155
C	PRO156
C	PHE157
C	LYS181
C	THR183
C	GLU184
C	GLY218
C	PHE232
C	GLY234
C	SER235
C	VAL238
C	LEU241
C	HOH775
C	HOH869

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE POA C 502

Chain	Residue
C	ARG108
C	HIS159
C	ARG290
C	CYS291
C	THR292
C	ARG447
C	HOH606
C	HOH698

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NAD D 501

Chain	Residue
D	ILE154
D	THR155
D	PRO156
D	PHE157
D	LYS181
D	THR183
D	GLU184
D	PRO214
D	GLY218
D	PHE232
D	SER235
D	VAL238
D	LEU241
D	HOH753
D	HOH758
D	HOH907

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POA D 502

Chain	Residue
D	ARG447
D	HOH628
D	HOH679
D	HOH909
D	ARG108
D	ASN158
D	HIS159
D	ARG290
D	CYS291
D	THR292

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NAD E 501

Chain	Residue
E	ILE154
E	THR155
E	PRO156
E	PHE157
E	LYS181
E	THR183
E	GLU184
E	GLY218
E	PHE232
E	SER235
E	VAL238
E	HOH776
E	HOH801
E	HOH897

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POA E 502

Chain	Residue
E	ARG108
E	ASN158
E	HIS159
E	ARG290
E	CYS291
E	THR292
E	ARG447
E	HOH620
E	HOH623
E	HOH764

site_id	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NAD F 501

Chain	Residue
F	ILE154
F	THR155
F	PRO156
F	PHE157
F	LYS181
F	THR183
F	GLU184
F	GLY218
F	PHE232
F	SER235
F	VAL238
F	HOH760
F	HOH770

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE POA F 502

Chain	Residue
F	ARG108
F	ASN158
F	HIS159
F	MET163
F	ARG290
F	CYS291
F	THR292
F	ARG447
F	HOH604

site_id	BC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAD G 501

Chain	Residue
G	ILE154
G	THR155
G	PRO156
G	PHE157
G	LYS181
G	THR183
G	GLU184
G	PRO214
G	GLY218
G	PHE232
G	SER235
G	VAL238
G	LEU241
G	HOH637
G	HOH722
G	HOH818
G	HOH849
G	HOH907

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POA G 502

Chain	Residue
G	ARG108
G	ASN158
G	HIS159
G	MET163
G	ARG290
G	CYS291
G	THR292
G	ARG447
G	HOH606
G	HOH610

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POA H 501

Chain	Residue
H	ARG108
H	ASN158
H	HIS159
H	GLU254
H	ARG290
H	CYS291
H	THR292
H	ARG447
H	HOH722
H	HOH819

Functional Information from PROSITE/UniProt

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGNDP

Chain	Residue	Details
A	LEU253-PRO260

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24361046","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24361046","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24361046","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4I3X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24361046","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4I3V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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