6RTU
Piperideine-6-carboxylate dehydrogenase from Streptomyces clavuligerus complexed with alpha-aminoadipic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004029 | molecular_function | 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 | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004029 | molecular_function | 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 | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue UN1 A 601 |
| Chain | Residue |
| A | GLU118 |
| A | PHE468 |
| A | HOH720 |
| A | HOH892 |
| B | HOH835 |
| A | ASN164 |
| A | PHE165 |
| A | ARG298 |
| A | CYS299 |
| A | THR300 |
| A | SER460 |
| A | GLY461 |
| A | ALA462 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 602 |
| Chain | Residue |
| A | ASP412 |
| A | LEU413 |
| A | ARG441 |
| A | HOH735 |
| A | HOH767 |
| A | HOH791 |
| A | HOH795 |
| A | HOH831 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | THR393 |
| A | ALA394 |
| A | ARG397 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | GLN371 |
| A | ARG383 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | ARG22 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | ILE6 |
| A | GLY8 |
| A | ARG501 |
| A | THR503 |
| A | LEU504 |
| A | HOH708 |
| A | HOH725 |
| A | HOH889 |
| A | HOH922 |
| A | HOH942 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 607 |
| Chain | Residue |
| A | ARG38 |
| A | GLY43 |
| A | ASN343 |
| A | GLU344 |
| A | ALA345 |
| A | HOH739 |
| A | HOH915 |
| A | HOH987 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 608 |
| Chain | Residue |
| A | GLU471 |
| A | LYS472 |
| A | HOH758 |
| A | HOH798 |
| A | HOH986 |
| B | LEU154 |
| B | ARG490 |
| B | HOH1083 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 701 |
| Chain | Residue |
| B | ASP412 |
| B | LEU413 |
| B | ARG441 |
| B | HOH817 |
| B | HOH831 |
| B | HOH873 |
| B | HOH909 |
| B | HOH1044 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 702 |
| Chain | Residue |
| B | THR393 |
| B | ALA394 |
| B | ARG397 |
| B | ARG418 |
| B | HOH979 |
| B | HOH1020 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 703 |
| Chain | Residue |
| B | GLN371 |
| B | ARG383 |
| B | HOH839 |
| B | HOH913 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 704 |
| Chain | Residue |
| B | LEU504 |
| B | VAL508 |
| B | ASP509 |
| B | PHE510 |
| B | SER511 |
| B | HOH841 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 705 |
| Chain | Residue |
| A | GLY476 |
| A | ARG478 |
| B | TRP151 |
| B | ARG491 |
| B | HOH801 |
| B | HOH821 |
| B | HOH968 |
| B | HOH1026 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 706 |
| Chain | Residue |
| B | ARG38 |
| B | GLY43 |
| B | ASN343 |
| B | GLU344 |
| B | ALA345 |
| B | HOH844 |
| B | HOH898 |
| B | HOH1088 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 707 |
| Chain | Residue |
| A | LEU154 |
| A | HOH907 |
| B | GLU471 |
| B | LYS472 |
| B | HOH881 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 708 |
| Chain | Residue |
| B | TRP172 |
| B | ALA462 |
| B | GLU463 |
| B | ILE464 |
| B | GLY466 |
| B | PHE468 |
| B | SER480 |
| B | HOH803 |
| B | GLU118 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 709 |
| Chain | Residue |
| B | THR409 |
| B | ARG411 |
| B | HOH981 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGNNA |
| Chain | Residue | Details |
| A | LEU264-ALA271 |
