5J84
Crystal structure of L-arabinonate dehydratase in holo-form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008869 | molecular_function | galactonate dehydratase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0047818 | molecular_function | D-fuconate dehydratase activity |
| A | 0050020 | molecular_function | L-arabinonate dehydratase activity |
| B | 0008869 | molecular_function | galactonate dehydratase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0047818 | molecular_function | D-fuconate dehydratase activity |
| B | 0050020 | molecular_function | L-arabinonate dehydratase activity |
| C | 0008869 | molecular_function | galactonate dehydratase activity |
| C | 0016836 | molecular_function | hydro-lyase activity |
| C | 0047818 | molecular_function | D-fuconate dehydratase activity |
| C | 0050020 | molecular_function | L-arabinonate dehydratase activity |
| D | 0008869 | molecular_function | galactonate dehydratase activity |
| D | 0016836 | molecular_function | hydro-lyase activity |
| D | 0047818 | molecular_function | D-fuconate dehydratase activity |
| D | 0050020 | molecular_function | L-arabinonate dehydratase activity |
| E | 0008869 | molecular_function | galactonate dehydratase activity |
| E | 0016836 | molecular_function | hydro-lyase activity |
| E | 0047818 | molecular_function | D-fuconate dehydratase activity |
| E | 0050020 | molecular_function | L-arabinonate dehydratase activity |
| F | 0008869 | molecular_function | galactonate dehydratase activity |
| F | 0016836 | molecular_function | hydro-lyase activity |
| F | 0047818 | molecular_function | D-fuconate dehydratase activity |
| F | 0050020 | molecular_function | L-arabinonate dehydratase activity |
| G | 0008869 | molecular_function | galactonate dehydratase activity |
| G | 0016836 | molecular_function | hydro-lyase activity |
| G | 0047818 | molecular_function | D-fuconate dehydratase activity |
| G | 0050020 | molecular_function | L-arabinonate dehydratase activity |
| H | 0008869 | molecular_function | galactonate dehydratase activity |
| H | 0016836 | molecular_function | hydro-lyase activity |
| H | 0047818 | molecular_function | D-fuconate dehydratase activity |
| H | 0050020 | molecular_function | L-arabinonate dehydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | GLU91 |
| A | ASP128 |
| A | KCX129 |
| A | GLU453 |
| A | HOH769 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue FES A 602 |
| Chain | Residue |
| A | THR199 |
| A | CYS200 |
| A | ALA206 |
| B | TYR26 |
| A | CYS59 |
| A | ASN92 |
| A | CYS127 |
| A | ASP128 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 601 |
| Chain | Residue |
| B | GLU91 |
| B | ASP128 |
| B | KCX129 |
| B | THR205 |
| B | ASN278 |
| B | GLU453 |
| B | HOH814 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue FES B 602 |
| Chain | Residue |
| A | TYR26 |
| A | TRP30 |
| B | CYS59 |
| B | ASN92 |
| B | CYS127 |
| B | ASP128 |
| B | CYS200 |
| B | HOH838 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MG C 601 |
| Chain | Residue |
| C | GLU91 |
| C | ASP128 |
| C | KCX129 |
| C | THR205 |
| C | ASN278 |
| C | GLU453 |
| C | HOH719 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue FES C 602 |
| Chain | Residue |
| C | CYS59 |
| C | CYS127 |
| C | THR199 |
| C | CYS200 |
| D | TYR26 |
| D | TRP30 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 601 |
| Chain | Residue |
| D | GLU91 |
| D | ASP128 |
| D | KCX129 |
| D | THR205 |
| D | GLU453 |
| D | HOH816 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue FES D 602 |
| Chain | Residue |
| C | TRP30 |
| D | CYS59 |
| D | CYS127 |
| D | ASP128 |
| D | CYS200 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MG E 601 |
| Chain | Residue |
| E | GLU91 |
| E | ASP128 |
| E | KCX129 |
| E | THR205 |
| E | GLU453 |
| E | HOH785 |
| E | HOH790 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue FES E 602 |
| Chain | Residue |
| E | CYS59 |
| E | ASN92 |
| E | CYS127 |
| E | ASP128 |
| E | CYS200 |
| F | TYR26 |
| F | TRP30 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG F 601 |
| Chain | Residue |
| F | GLU91 |
| F | ASP128 |
| F | KCX129 |
| F | GLU453 |
| F | HOH729 |
| F | HOH758 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue FES F 602 |
| Chain | Residue |
| E | TRP30 |
| F | CYS59 |
| F | ASN92 |
| F | CYS127 |
| F | ASP128 |
| F | THR199 |
| F | CYS200 |
| F | ALA206 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue MG G 601 |
| Chain | Residue |
| G | GLU91 |
| G | ASP128 |
| G | KCX129 |
| G | GLU453 |
| G | HOH788 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue FES G 602 |
| Chain | Residue |
| G | CYS59 |
| G | ASN92 |
| G | CYS127 |
| G | ASP128 |
| G | CYS200 |
| G | ALA206 |
| H | TYR26 |
| H | TRP30 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue MG H 601 |
| Chain | Residue |
| H | GLU91 |
| H | ASP128 |
| H | KCX129 |
| H | GLU453 |
| H | HOH715 |
| H | HOH787 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue FES H 602 |
| Chain | Residue |
| G | TYR26 |
| H | CYS59 |
| H | ASN92 |
| H | CYS127 |
| H | ASP128 |
| H | CYS200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28574691","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






