1PS9
The Crystal Structure and Reaction Mechanism of E. coli 2,4-Dienoyl CoA Reductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0033543 | biological_process | fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 705 |
| Chain | Residue |
| A | SER406 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 706 |
| Chain | Residue |
| A | ASN75 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 707 |
| Chain | Residue |
| A | HIS361 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 700 |
| Chain | Residue |
| A | CYS341 |
| A | CYS353 |
| A | LEU354 |
| A | ARG311 |
| A | CYS334 |
| A | ILE335 |
| A | CYS337 |
| A | ASN338 |
| A | ALA340 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD A 701 |
| Chain | Residue |
| A | GLN339 |
| A | LEU354 |
| A | GLY380 |
| A | GLY382 |
| A | PRO383 |
| A | ALA384 |
| A | ASP403 |
| A | ALA404 |
| A | HIS405 |
| A | GLY410 |
| A | GLN411 |
| A | PHE412 |
| A | ILE414 |
| A | ALA415 |
| A | LYS421 |
| A | PHE424 |
| A | HIS446 |
| A | VAL448 |
| A | ALA462 |
| A | SER463 |
| A | GLY464 |
| A | LEU487 |
| A | ASP508 |
| A | ASN629 |
| A | GLY647 |
| A | GLY648 |
| A | LEU655 |
| A | ASP656 |
| A | ALA657 |
| A | NAP703 |
| A | HOH787 |
| A | HOH961 |
| A | HOH1026 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN A 702 |
| Chain | Residue |
| A | SER24 |
| A | MET25 |
| A | HIS26 |
| A | GLY58 |
| A | GLN100 |
| A | MET161 |
| A | ARG214 |
| A | THR286 |
| A | ASN287 |
| A | ARG288 |
| A | MET309 |
| A | ALA310 |
| A | ARG311 |
| A | CYS341 |
| A | MDE704 |
| A | HOH708 |
| A | HOH709 |
| A | HOH949 |
| A | HOH956 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP A 703 |
| Chain | Residue |
| A | GLN339 |
| A | ARG468 |
| A | GLY504 |
| A | ILE505 |
| A | GLN561 |
| A | ARG562 |
| A | LYS563 |
| A | LEU571 |
| A | TYR596 |
| A | CYS623 |
| A | ALA624 |
| A | GLY625 |
| A | MET653 |
| A | GLU654 |
| A | LEU655 |
| A | ASP656 |
| A | FAD701 |
| A | HOH721 |
| A | HOH777 |
| A | HOH918 |
| A | HOH967 |
| A | HOH968 |
| A | HOH974 |
| A | HOH975 |
| A | HOH985 |
| site_id | AC8 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE MDE A 704 |
| Chain | Residue |
| A | THR258 |
| A | ILE259 |
| A | PHE346 |
| A | LYS566 |
| A | LYS573 |
| A | THR574 |
| A | TRP577 |
| A | FMN702 |
| A | HOH709 |
| A | HOH710 |
| A | HOH715 |
| A | HOH749 |
| A | HOH762 |
| A | HOH792 |
| A | HOH818 |
| A | HOH952 |
| A | HOH976 |
| A | HOH977 |
| A | HOH984 |
| A | HOH1045 |
| A | HIS26 |
| A | LEU102 |
| A | THR104 |
| A | PRO122 |
| A | GLU164 |
| A | TYR166 |
| A | ARG175 |
| A | HIS252 |
| A | GLU253 |
| A | ARG255 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12840019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18171025","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 23 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12840019","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PS9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12840019","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1PS9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity, assists active site Tyr in protonation of C4","evidences":[{"source":"PubMed","id":"12840019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18171025","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12840019 |
| Chain | Residue | Details |
| A | TYR166 | |
| A | HIS252 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 108 |
| Chain | Residue | Details |
| A | GLU164 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR166 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG214 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS252 | electrostatic stabiliser, hydrogen bond donor |
| A | GLN339 | hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
