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 | ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000269|PubMed:24361046 |
Chain | Residue | Details |
A | GLU254 | |
B | GLU254 | |
C | GLU254 | |
D | GLU254 | |
E | GLU254 | |
F | GLU254 | |
G | GLU254 | |
H | GLU254 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:24361046 |
Chain | Residue | Details |
A | CYS291 | |
B | CYS291 | |
C | CYS291 | |
D | CYS291 | |
E | CYS291 | |
F | CYS291 | |
G | CYS291 | |
H | CYS291 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24361046, ECO:0007744|PDB:4I3X |
Chain | Residue | Details |
A | ARG108 | |
B | ARG447 | |
C | ARG108 | |
C | HIS159 | |
C | ARG290 | |
C | GLU385 | |
C | ARG447 | |
D | ARG108 | |
D | HIS159 | |
D | ARG290 | |
D | GLU385 | |
A | HIS159 | |
D | ARG447 | |
E | ARG108 | |
E | HIS159 | |
E | ARG290 | |
E | GLU385 | |
E | ARG447 | |
F | ARG108 | |
F | HIS159 | |
F | ARG290 | |
F | GLU385 | |
A | ARG290 | |
F | ARG447 | |
G | ARG108 | |
G | HIS159 | |
G | ARG290 | |
G | GLU385 | |
G | ARG447 | |
H | ARG108 | |
H | HIS159 | |
H | ARG290 | |
H | GLU385 | |
A | GLU385 | |
H | ARG447 | |
A | ARG447 | |
B | ARG108 | |
B | HIS159 | |
B | ARG290 | |
B | GLU385 |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24361046, ECO:0007744|PDB:4I3V, ECO:0007744|PDB:4I3W, ECO:0007744|PDB:4I3X |
Chain | Residue | Details |
A | THR155 | |
D | THR155 | |
D | LYS181 | |
D | SER235 | |
E | THR155 | |
E | LYS181 | |
E | SER235 | |
F | THR155 | |
F | LYS181 | |
F | SER235 | |
G | THR155 | |
A | LYS181 | |
G | LYS181 | |
G | SER235 | |
H | THR155 | |
H | LYS181 | |
H | SER235 | |
A | SER235 | |
B | THR155 | |
B | LYS181 | |
B | SER235 | |
C | THR155 | |
C | LYS181 | |
C | SER235 |