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 | 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 | ACT_SITE: Proton donor => ECO:0000305|PubMed:12840019, ECO:0000305|PubMed:18171025 |
Chain | Residue | Details |
A | LEU167 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12840019, ECO:0007744|PDB:1PS9 |
Chain | Residue | Details |
A | MET25 | |
A | LEU342 | |
A | LEU354 | |
A | GLY385 | |
A | ALA404 | |
A | PHE412 | |
A | GLU422 | |
A | THR449 | |
A | LYS563 | |
A | CYS649 | |
A | GLU654 | |
A | ILE59 | |
A | ASP656 | |
A | ILE101 | |
A | LEU215 | |
A | ILE289 | |
A | ARG311 | |
A | ILE335 | |
A | ASN338 | |
A | ALA340 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:12840019, ECO:0007744|PDB:1PS9 |
Chain | Residue | Details |
A | THR176 | |
A | GLU253 | |
A | PRO567 | |
A | ILE578 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity, assists active site Tyr in protonation of C4 => ECO:0000305|PubMed:12840019, ECO:0000305|PubMed:18171025 |
Chain | Residue | Details |
A | GLU253 |
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 | GLY165 | electrostatic stabiliser, hydrogen bond donor |
A | LEU167 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | LEU215 | electrostatic stabiliser, hydrogen bond donor |
A | GLU253 | electrostatic stabiliser, hydrogen bond donor |
A | ALA340 | hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |