6BJP
Apo form of the E124S mutant of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008802 | molecular_function | betaine-aldehyde 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 |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008802 | molecular_function | betaine-aldehyde 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 |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008802 | molecular_function | betaine-aldehyde 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 |
| C | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008802 | molecular_function | betaine-aldehyde 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 |
| D | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue K A 501 |
| Chain | Residue |
| A | THR26 |
| A | ILE27 |
| A | ASP93 |
| A | VAL180 |
| A | HOH690 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| C | GLU5 |
| C | GLU6 |
| C | GLN7 |
| C | LYS8 |
| C | TYR15 |
| A | LEU307 |
| A | LEU352 |
| A | CYS353 |
| A | HOH732 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | GLN311 |
| C | PHE4 |
| C | GLN7 |
| C | LYS187 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | TYR115 |
| A | ALA449 |
| A | LYS457 |
| A | GLN458 |
| A | SER459 |
| A | GLY460 |
| A | VAL461 |
| A | HOH707 |
| A | HOH709 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | GLU482 |
| D | ARG269 |
| D | ASN442 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | GLN7 |
| A | LYS187 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | HOH681 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue K B 501 |
| Chain | Residue |
| B | THR26 |
| B | ILE27 |
| B | ASP93 |
| B | VAL180 |
| B | HOH635 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | GLY339 |
| B | TYR340 |
| B | GLU386 |
| B | HOH681 |
| B | HOH683 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | TYR116 |
| B | TRP161 |
| B | PRO165 |
| B | ALA449 |
| B | THR469 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | GLN7 |
| B | LYS187 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | GLU387 |
| B | HOH715 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | GLY445 |
| B | GLY455 |
| B | TYR456 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue K C 501 |
| Chain | Residue |
| C | THR26 |
| C | ILE27 |
| C | ASP93 |
| C | VAL180 |
| C | HOH723 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue K D 501 |
| Chain | Residue |
| D | THR26 |
| D | ILE27 |
| D | ASP93 |
| D | VAL180 |
| D | HOH643 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfSSGQVCTNGT |
| Chain | Residue | Details |
| A | PHE279-THR290 | |
| C | PHE279-THR290 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGKSP |
| Chain | Residue | Details |
| A | MET251-PRO258 | |
| C | MET251-PRO258 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:19013472 |
| Chain | Residue | Details |
| C | LYS162 | |
| C | GLU464 | |
| D | LYS162 | |
| D | GLU464 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:19013472 |
| Chain | Residue | Details |
| C | GLU252 | |
| D | GLU252 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:21732915 |
| Chain | Residue | Details |
| C | CYS286 | |
| D | CYS286 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| C | THR26 | |
| D | ASP93 | |
| D | VAL180 | |
| D | LEU246 | |
| D | LYS457 | |
| D | GLY460 | |
| C | ILE27 | |
| C | ASP93 | |
| C | VAL180 | |
| C | LEU246 | |
| C | LYS457 | |
| C | GLY460 | |
| D | THR26 | |
| D | ILE27 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21732915, ECO:0007744|PDB:2WOX |
| Chain | Residue | Details |
| C | GLY150 | |
| D | GLU387 | |
| C | LYS176 | |
| C | GLY209 | |
| C | GLY230 | |
| C | GLU387 | |
| D | GLY150 | |
| D | LYS176 | |
| D | GLY209 | |
| D | GLY230 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: covalent => ECO:0000269|PubMed:21732915, ECO:0007744|PDB:2WOX |
| Chain | Residue | Details |
| C | CYS286 | |
| D | CYS286 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Seems to be a necessary countercharge to the potassium cations |
| Chain | Residue | Details |
| C | GLU248 | |
| D | GLU248 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:19013472 |
| Chain | Residue | Details |
| C | CYS286 | |
| D | CYS286 |
