4F2D
Crystal Structure of Escherichia coli L-arabinose Isomerase (ECAI) complexed with Ribitol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005996 | biological_process | monosaccharide metabolic process |
| A | 0008733 | molecular_function | L-arabinose isomerase activity |
| A | 0016861 | molecular_function | intramolecular oxidoreductase activity, interconverting aldoses and ketoses |
| A | 0019568 | biological_process | arabinose catabolic process |
| A | 0019569 | biological_process | L-arabinose catabolic process to D-xylulose 5-phosphate |
| A | 0030145 | molecular_function | manganese ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005996 | biological_process | monosaccharide metabolic process |
| B | 0008733 | molecular_function | L-arabinose isomerase activity |
| B | 0016861 | molecular_function | intramolecular oxidoreductase activity, interconverting aldoses and ketoses |
| B | 0019568 | biological_process | arabinose catabolic process |
| B | 0019569 | biological_process | L-arabinose catabolic process to D-xylulose 5-phosphate |
| B | 0030145 | molecular_function | manganese ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005996 | biological_process | monosaccharide metabolic process |
| C | 0008733 | molecular_function | L-arabinose isomerase activity |
| C | 0016861 | molecular_function | intramolecular oxidoreductase activity, interconverting aldoses and ketoses |
| C | 0019568 | biological_process | arabinose catabolic process |
| C | 0019569 | biological_process | L-arabinose catabolic process to D-xylulose 5-phosphate |
| C | 0030145 | molecular_function | manganese ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 601 |
| Chain | Residue |
| A | GLU306 |
| A | GLU333 |
| A | HIS350 |
| A | HIS450 |
| A | RB0602 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE RB0 A 602 |
| Chain | Residue |
| A | TYR335 |
| A | HIS449 |
| A | HIS450 |
| A | MN601 |
| A | HOH788 |
| B | GLN16 |
| B | LEU18 |
| B | TYR19 |
| B | PHE83 |
| B | GLN125 |
| B | HIS128 |
| A | MSE185 |
| A | PHE279 |
| A | GLU306 |
| A | GLU333 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 601 |
| Chain | Residue |
| B | GLU306 |
| B | GLU333 |
| B | HIS350 |
| B | HIS450 |
| B | RB0602 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE RB0 B 602 |
| Chain | Residue |
| B | MSE185 |
| B | PHE279 |
| B | GLU306 |
| B | GLU333 |
| B | HIS449 |
| B | HIS450 |
| B | MN601 |
| B | HOH776 |
| C | GLN16 |
| C | TYR19 |
| C | PHE83 |
| C | GLN125 |
| C | HIS128 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY B 603 |
| Chain | Residue |
| A | TRP491 |
| A | VAL494 |
| B | TRP491 |
| B | VAL494 |
| C | TRP491 |
| C | VAL494 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 601 |
| Chain | Residue |
| C | GLU306 |
| C | GLU333 |
| C | HIS350 |
| C | HIS450 |
| C | RB0602 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RB0 C 602 |
| Chain | Residue |
| A | GLN125 |
| A | HIS128 |
| C | MSE185 |
| C | PHE279 |
| C | GLU306 |
| C | GLU333 |
| C | HIS449 |
| C | HIS450 |
| C | MN601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Binding site: {} |
| Chain | Residue | Details |
