Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4I3X

Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetate 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	30
Details	BINDING SITE FOR RESIDUE NAD A 501

Chain	Residue
A	ILE154
A	GLY218
A	PHE232
A	THR233
A	GLY234
A	SER235
A	VAL238
A	GLU254
A	LEU255
A	GLY256
A	GLY257
A	THR155
A	CYS291
A	GLU385
A	PHE387
A	PHE453
A	PAE502
A	HOH686
A	HOH720
A	HOH834
A	HOH935
A	HOH947
A	PRO156
A	HOH1004
A	PHE157
A	ASN158
A	LYS181
A	THR183
A	GLU184
A	PRO214

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PAE A 502

Chain	Residue
A	ARG108
A	ASN158
A	HIS159
A	ARG290
A	CYS291
A	THR292
A	ARG447
A	NAD501
A	HOH627
A	HOH719
A	HOH723
A	HOH1070

site_id	AC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAD B 501

Chain	Residue
B	ILE154
B	THR155
B	PRO156
B	PHE157
B	ASN158
B	LYS181
B	THR183
B	GLU184
B	PRO214
B	GLY218
B	PHE232
B	THR233
B	GLY234
B	SER235
B	VAL238
B	GLU254
B	LEU255
B	GLY256
B	GLY257
B	CYS291
B	GLU385
B	PHE387
B	PHE453
B	PAE502
B	HOH632
B	HOH676
B	HOH843
B	HOH899

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PAE B 502

Chain	Residue
B	ARG108
B	ASN158
B	HIS159
B	ARG290
B	CYS291
B	ARG447
B	NAD501
B	HOH621
B	HOH648
B	HOH961
B	HOH978

site_id	AC5
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD C 501

Chain	Residue
C	GLY257
C	CYS291
C	GLU385
C	PHE387
C	PHE453
C	PAE502
C	HOH642
C	HOH702
C	HOH713
C	HOH770
C	HOH779
C	HOH929
C	ILE154
C	THR155
C	PRO156
C	PHE157
C	ASN158
C	LYS181
C	THR183
C	GLU184
C	PRO214
C	GLY218
C	PHE232
C	THR233
C	GLY234
C	SER235
C	VAL238
C	GLU254
C	LEU255
C	GLY256

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PAE C 502

Chain	Residue
C	ARG108
C	ASN158
C	HIS159
C	ARG290
C	CYS291
C	THR292
C	ARG447
C	NAD501
C	HOH606

site_id	AC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAD D 501

Chain	Residue
D	ILE154
D	THR155
D	PRO156
D	PHE157
D	ASN158
D	LYS181
D	THR183
D	GLU184
D	PRO214
D	GLY218
D	PHE232
D	THR233
D	GLY234
D	SER235
D	VAL238
D	LEU241
D	GLU254
D	LEU255
D	GLY256
D	GLY257
D	CYS291
D	GLU385
D	PHE387
D	PHE453
D	PAE502
D	HOH645
D	HOH700
D	HOH807

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PAE D 502

Chain	Residue
D	ARG108
D	ASN158
D	HIS159
D	ARG290
D	CYS291
D	ARG447
D	NAD501
D	HOH624
D	HOH719

site_id	AC9
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAD E 501

Chain	Residue
E	ILE154
E	THR155
E	PRO156
E	PHE157
E	ASN158
E	LYS181
E	THR183
E	GLU184
E	GLY218
E	PHE232
E	THR233
E	GLY234
E	SER235
E	VAL238
E	LEU241
E	GLU254
E	LEU255
E	GLY256
E	GLY257
E	CYS291
E	GLU385
E	PHE387
E	PHE453
E	PAE502
E	HOH644
E	HOH691
E	HOH765
E	HOH783
E	HOH793

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

Chain	Residue
E	ARG108
E	ASN158
E	HIS159
E	ARG290
E	CYS291
E	THR292
E	ARG447
E	NAD501
E	HOH628
E	HOH679

site_id	BC2
Number of Residues	27
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	THR233
F	GLY234
F	SER235
F	VAL238
F	LEU241
F	GLU254
F	LEU255
F	GLY256
F	GLY257
F	CYS291
F	GLU385
F	PHE387
F	PHE453
F	PAE502
F	HOH617
F	HOH724
F	HOH821
F	HOH826

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PAE F 502

Chain	Residue
F	ARG108
F	ASN158
F	HIS159
F	ARG290
F	CYS291
F	THR292
F	ARG447
F	NAD501
F	HOH675
F	HOH758
F	HOH775

site_id	BC4
Number of Residues	28
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	THR233
G	GLY234
G	SER235
G	VAL238
G	LEU241
G	GLU254
G	LEU255
G	GLY256
G	GLY257
G	CYS291
G	GLU385
G	PHE387
G	PHE453
G	PAE502
G	HOH695
G	HOH844
G	HOH897
G	HOH932

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

Chain	Residue
G	ARG108
G	HIS159
G	ARG290
G	CYS291
G	THR292
G	ARG447
G	NAD501
G	HOH624
G	HOH696
G	HOH760

site_id	BC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD H 501

Chain	Residue
H	ILE154
H	THR155
H	PRO156
H	PHE157
H	ASN158
H	LYS181
H	THR183
H	GLU184
H	GLY218
H	PHE232
H	THR233
H	GLY234
H	SER235
H	VAL238
H	LEU241
H	GLU254
H	LEU255
H	GLY256
H	GLY257
H	CYS291
H	GLU385
H	PHE387
H	PHE453
H	PAE502
H	HOH669
H	HOH716

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PAE H 502

Chain	Residue
H	ARG108
H	ASN158
H	HIS159
H	ARG290
H	CYS291
H	ARG447
H	NAD501
H	HOH668
H	HOH833

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)