6I5G
X-ray structure of human soluble Epoxide Hydrolase C-terminal Domain (hsEH CTD)in complex with 15d-PGJ2
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 601 |
| Chain | Residue |
| A | GLU269 |
| A | SER273 |
| A | HIS334 |
| A | TRP525 |
| A | THR526 |
| A | GLN527 |
| A | MET528 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 602 |
| Chain | Residue |
| A | LEU313 |
| A | GLU316 |
| A | MET317 |
| A | MET293 |
| A | LYS294 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 603 |
| Chain | Residue |
| A | GLU269 |
| A | SER270 |
| A | ASP292 |
| A | TYR296 |
| A | GLY297 |
| A | GLN453 |
| A | PHE454 |
| A | HOH748 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 604 |
| Chain | Residue |
| A | PRO390 |
| A | GLY391 |
| A | ARG460 |
| A | HOH709 |
| A | HOH758 |
| B | PRO302 |
| B | GLU304 |
| B | GLU307 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 605 |
| Chain | Residue |
| A | ASN468 |
| A | MET469 |
| A | GLU470 |
| A | ARG471 |
| A | HOH751 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 606 |
| Chain | Residue |
| A | VAL318 |
| A | GLU350 |
| A | ARG351 |
| A | HOH712 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue PTG A 607 |
| Chain | Residue |
| A | PHE387 |
| A | LEU408 |
| A | SER412 |
| A | SER415 |
| A | MET419 |
| A | LYS495 |
| A | ASP496 |
| A | PHE497 |
| A | VAL498 |
| A | HIS524 |
| A | HOH790 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 601 |
| Chain | Residue |
| B | MET293 |
| B | LYS294 |
| B | LEU313 |
| B | GLU316 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 602 |
| Chain | Residue |
| A | SER238 |
| A | GLY240 |
| A | PHE252 |
| A | GLU254 |
| B | SER238 |
| B | GLY240 |
| B | PHE252 |
| B | GLU254 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 603 |
| Chain | Residue |
| B | ALA345 |
| B | LEU346 |
| B | PRO349 |
| B | ASP413 |
| B | LYS483 |
| B | LEU485 |
| B | HOH716 |
| B | HOH737 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 604 |
| Chain | Residue |
| B | HIS239 |
| B | HIS251 |
| B | TRP271 |
| B | ASP292 |
| B | GLU298 |
| B | GLN453 |
| B | HOH763 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 605 |
| Chain | Residue |
| B | LYS315 |
| B | THR319 |
| B | GLU494 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 606 |
| Chain | Residue |
| B | SER257 |
| B | GLY258 |
| B | GLY285 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue PTG B 607 |
| Chain | Residue |
| B | TYR383 |
| B | PHE387 |
| B | SER412 |
| B | SER415 |
| B | MET419 |
| B | LYS495 |
| B | ASP496 |
| B | PHE497 |
| B | VAL498 |
| B | HIS524 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 |
| Chain | Residue | Details |
| A | GLN388 | |
| B | GLN388 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 |
| Chain | Residue | Details |
| A | ILE519 | |
| B | ILE519 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15096040 |
| Chain | Residue | Details |
| A | SER238 | |
| B | SER238 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 |
| Chain | Residue | Details |
| A | PRO436 | |
| B | PRO436 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P34914 |
| Chain | Residue | Details |
| A | VAL244 | |
| A | PRO268 | |
| B | VAL244 | |
| B | PRO268 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P34914 |
| Chain | Residue | Details |
| A | CYS423 | |
| B | CYS423 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P34914 |
| Chain | Residue | Details |
| A | LYS474 | |
| A | GLU508 | |
| B | LYS474 | |
| B | GLU508 |
