6U7L
2.75 Angstrom Crystal Structure of Galactarate Dehydratase from Escherichia coli.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008867 | molecular_function | galactarate dehydratase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019698 | biological_process | D-galacturonate catabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046392 | biological_process | galactarate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0008867 | molecular_function | galactarate dehydratase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019698 | biological_process | D-galacturonate catabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046392 | biological_process | galactarate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008198 | molecular_function | ferrous iron binding |
| C | 0008867 | molecular_function | galactarate dehydratase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019698 | biological_process | D-galacturonate catabolic process |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046392 | biological_process | galactarate catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008198 | molecular_function | ferrous iron binding |
| D | 0008867 | molecular_function | galactarate dehydratase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019698 | biological_process | D-galacturonate catabolic process |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046392 | biological_process | galactarate catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 601 |
| Chain | Residue |
| A | GLN287 |
| A | CYS288 |
| A | GLU321 |
| A | ALA417 |
| A | ASP419 |
| A | HOH720 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CA A 602 |
| Chain | Residue |
| A | GLN507 |
| A | HOH735 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CA A 603 |
| Chain | Residue |
| A | GLU479 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 604 |
| Chain | Residue |
| A | ASN338 |
| A | GLU340 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 605 |
| Chain | Residue |
| A | GLU397 |
| A | VAL398 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 606 |
| Chain | Residue |
| A | ASN197 |
| A | GLN403 |
| A | ARG404 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 607 |
| Chain | Residue |
| A | HIS491 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 601 |
| Chain | Residue |
| B | GLN287 |
| B | CYS288 |
| B | GLU321 |
| B | ALA417 |
| B | ASP419 |
| B | HOH710 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue CA B 602 |
| Chain | Residue |
| B | GLU479 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 601 |
| Chain | Residue |
| C | GLN287 |
| C | CYS288 |
| C | GLU321 |
| C | ALA417 |
| C | ASP419 |
| C | HOH708 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue CA C 602 |
| Chain | Residue |
| C | GLU479 |
| C | HOH705 |
| C | HOH743 |
| C | HOH746 |
| C | HOH749 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 601 |
| Chain | Residue |
| D | GLN287 |
| D | CYS288 |
| D | GLU321 |
| D | ALA417 |
| D | ASP419 |
| D | HOH702 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue CA D 602 |
| Chain | Residue |
| D | GLU479 |
| D | HOH709 |
| D | HOH723 |
| D | HOH732 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 604 |
| Chain | Residue |
| D | VAL398 |
| site_id | AD6 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 605 |
| Chain | Residue |
| D | ASN197 |
Functional Information from PROSITE/UniProt
| site_id | PS00430 |
| Number of Residues | 98 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. snamanieirqetptafyikvhdtdnvaiivndnglkagtrfpdgleliehipqghkvalldipangeiirygevigyavraiprgswid.........................ESMVVLPE |
| Chain | Residue | Details |
| A | SER-2-GLU95 | |
| C | SER-2-GLU95 |
