5L78
Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain (in NAD+ bound form)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 1001 |
| Chain | Residue |
| A | CYS633 |
| A | GLY635 |
| A | ARG726 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 1002 |
| Chain | Residue |
| A | ILE924 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 1003 |
| Chain | Residue |
| A | SER868 |
| A | GLU832 |
| A | LYS833 |
| A | ASP834 |
| A | GLY862 |
| A | ASP863 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | binding site for residue NAD A 1004 |
| Chain | Residue |
| A | GLY487 |
| A | SER488 |
| A | GLY489 |
| A | ILE491 |
| A | SER511 |
| A | ASP512 |
| A | MET513 |
| A | GLN516 |
| A | MET531 |
| A | ASP532 |
| A | ILE533 |
| A | LEU553 |
| A | LEU554 |
| A | PRO555 |
| A | LEU558 |
| A | HIS559 |
| A | ALA576 |
| A | SER577 |
| A | LEU601 |
| A | LEU603 |
| A | ASP604 |
| A | PRO605 |
| A | TRP652 |
| A | VAL874 |
| A | HOH1143 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | binding site for residue NAD B 1001 |
| Chain | Residue |
| B | SER488 |
| B | GLY489 |
| B | ILE491 |
| B | SER511 |
| B | ASP512 |
| B | MET513 |
| B | GLN516 |
| B | MET531 |
| B | ASP532 |
| B | ILE533 |
| B | LEU553 |
| B | LEU554 |
| B | PRO555 |
| B | TYR556 |
| B | LEU558 |
| B | ALA576 |
| B | SER577 |
| B | LEU601 |
| B | LEU603 |
| B | ASP604 |
| B | PRO605 |
| B | VAL874 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2016","submissionDatabase":"PDB data bank","title":"Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain (in NAD+ bound form).","authors":["Kopec J.","Yue W.W."]}},{"source":"PDB","id":"5L78","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9P4R4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99K67","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99K67","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99K67","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
