3K2W
CRYSTAL STRUCTURE OF betaine-aldehyde dehydrogenase FROM Pseudoalteromonas atlantica T6c
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 496 |
| Chain | Residue |
| A | ALA69 |
| A | ARG72 |
| A | ALA123 |
| A | LYS144 |
| A | ILE172 |
| A | HOH698 |
| B | GOL497 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 497 |
| Chain | Residue |
| A | LEU418 |
| A | SER419 |
| A | LYS259 |
| A | ALA260 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 496 |
| Chain | Residue |
| A | ILE130 |
| A | PRO132 |
| B | ILE126 |
| B | GLY128 |
| B | HIS143 |
| B | LYS144 |
| B | HOH508 |
| B | HOH524 |
| B | HOH1231 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 497 |
| Chain | Residue |
| A | GLY128 |
| A | HIS143 |
| A | LYS144 |
| A | GOL496 |
| A | HOH509 |
| B | ILE130 |
| B | LEU131 |
| B | PRO132 |
| B | HOH517 |
| B | HOH1035 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 498 |
| Chain | Residue |
| B | ALA268 |
| B | ASP269 |
| B | HIS423 |
| B | GLN425 |
| B | ASN445 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 499 |
| Chain | Residue |
| B | TYR141 |
| B | ILE484 |
| B | GLU486 |
| C | PHE427 |
| C | ASN431 |
| D | HOH710 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 500 |
| Chain | Residue |
| B | LYS259 |
| B | ALA260 |
| B | LEU418 |
| B | SER419 |
| B | HOH1308 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 496 |
| Chain | Residue |
| C | LYS259 |
| C | ALA260 |
| C | LEU418 |
| C | SER419 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 497 |
| Chain | Residue |
| C | TYR302 |
| C | ASP379 |
| C | VAL380 |
| C | ILE398 |
| C | VAL399 |
| C | LYS400 |
| C | HOH1371 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT C 498 |
| Chain | Residue |
| C | ALA268 |
| C | ASP269 |
| C | HIS423 |
| C | GLN425 |
| C | ASN445 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT C 499 |
| Chain | Residue |
| C | ARG72 |
| C | ALA123 |
| C | ILE172 |
| C | THR173 |
| D | GOL497 |
| D | HOH1808 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 496 |
| Chain | Residue |
| C | ILE130 |
| C | PRO132 |
| D | ILE126 |
| D | GLY128 |
| D | HIS143 |
| D | LYS144 |
| D | GOL498 |
| D | HOH627 |
| D | HOH699 |
| D | HOH812 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 497 |
| Chain | Residue |
| C | GLY128 |
| C | LYS144 |
| C | ACT499 |
| C | HOH527 |
| D | ILE130 |
| D | PRO132 |
| D | HOH1185 |
| D | HOH1772 |
| D | HOH1808 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 498 |
| Chain | Residue |
| D | ALA69 |
| D | ARG72 |
| D | ALA123 |
| D | ILE172 |
| D | LEU477 |
| D | GOL496 |
| D | HOH549 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 499 |
| Chain | Residue |
| D | GLY258 |
| D | LYS259 |
| D | ALA260 |
| D | LEU418 |
| D | SER419 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT D 500 |
| Chain | Residue |
| D | ALA268 |
| D | ASP269 |
| D | LYS272 |
| D | HIS423 |
| D | THR424 |
| D | ASN445 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL E 496 |
| Chain | Residue |
| E | ILE126 |
| E | GLY128 |
| E | HIS143 |
| E | LYS144 |
| E | HOH561 |
| E | HOH872 |
| E | HOH1763 |
| F | ILE130 |
| F | PRO132 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 497 |
| Chain | Residue |
| E | PHE427 |
| E | ASN431 |
| F | PHE427 |
| F | ASN431 |
| G | TYR141 |
| G | HOH522 |
| H | HOH528 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL E 498 |
| Chain | Residue |
| E | GLY258 |
| E | LYS259 |
| E | ALA260 |
| E | LEU418 |
| E | SER419 |
| E | HOH697 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT E 499 |
| Chain | Residue |
| E | ALA268 |
| E | ASP269 |
| E | HIS423 |
| E | GLN425 |
| E | ASN445 |
| E | HOH1805 |
| site_id | CC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL F 496 |
| Chain | Residue |
| E | ILE130 |
| E | PRO132 |
| F | ILE126 |
| F | GLY128 |
| F | HIS143 |
| F | LYS144 |
| F | HOH504 |
| F | HOH537 |
| F | HOH1048 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL F 497 |
| Chain | Residue |
| F | LYS144 |
| F | GLU474 |
| F | HOH554 |
| H | LYS470 |
| H | PHE471 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL F 498 |
| Chain | Residue |
| F | GLY213 |
| F | GLY217 |
| F | GLN218 |
| F | HOH668 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL F 499 |
| Chain | Residue |
| F | LYS259 |
| F | ALA260 |
| F | LEU418 |
| F | SER419 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT F 500 |
| Chain | Residue |
| F | ALA268 |
| F | ASP269 |
| F | HIS423 |
| F | GLN425 |
| F | ASN445 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL G 496 |
| Chain | Residue |
| E | HOH573 |
| F | HOH552 |
| G | PHE427 |
| G | ASN431 |
| H | PHE427 |
| H | ASN431 |
| site_id | CC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL G 497 |
| Chain | Residue |
| G | ILE130 |
| G | PRO132 |
| G | HOH1080 |
| H | ILE126 |
| H | GLY128 |
| H | HIS143 |
| H | LYS144 |
| H | GOL496 |
| H | HOH498 |
| H | HOH509 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL G 498 |
| Chain | Residue |
| G | GLY128 |
| G | HIS143 |
| G | LYS144 |
| G | HOH561 |
| G | HOH1605 |
| H | ILE130 |
| H | PRO132 |
| site_id | DC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL G 499 |
| Chain | Residue |
| G | LYS259 |
| G | LEU418 |
| G | SER419 |
| G | HOH952 |
| site_id | DC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL H 496 |
| Chain | Residue |
| G | GOL497 |
| H | ARG72 |
| H | ALA123 |
| H | LYS144 |
| H | ILE172 |
| H | HOH1171 |
| site_id | DC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL H 497 |
| Chain | Residue |
| H | GLY258 |
| H | LYS259 |
| H | ALA260 |
| H | GLY417 |
| H | LEU418 |
| H | SER419 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FaNCGQVCTCVE |
| Chain | Residue | Details |
| A | PHE282-GLU293 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKAP |
| Chain | Residue | Details |
| A | LEU254-PRO261 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | CYS289 | |
| A | GLU255 | |
| A | ASN157 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | CYS289 | |
| B | GLU255 | |
| B | ASN157 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| C | CYS289 | |
| C | GLU255 | |
| C | ASN157 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| D | CYS289 | |
| D | GLU255 | |
| D | ASN157 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| E | CYS289 | |
| E | GLU255 | |
| E | ASN157 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| F | CYS289 | |
| F | GLU255 | |
| F | ASN157 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| G | CYS289 | |
| G | GLU255 | |
| G | ASN157 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| H | CYS289 | |
| H | GLU255 | |
| H | ASN157 |
