Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0009045 | molecular_function | xylose isomerase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042732 | biological_process | D-xylose metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0009045 | molecular_function | xylose isomerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042732 | biological_process | D-xylose metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | M1A |
| Number of Residues | 5 |
| Details | WHILE THE ACTIVE SITE IN THE WILD TYPE ENZYME CONTAINS THE METAL BINDING SITE, IN THIS MUTANT THE METAL IONS IN THESE SITES ARE REPLACED BY THE N-EPSILON AMINO GROUPS OF LYS |
| Chain | Residue |
| A | LYS180 |
| A | ASP244 |
| A | ASP286 |
| A | GLU216 |
| A | GLO950 |
| site_id | M1B |
| Number of Residues | 5 |
| Details | WHILE THE ACTIVE SITE IN THE WILD TYPE ENZYME CONTAINS THE METAL BINDING SITE, IN THIS MUTANT THE METAL IONS IN THESE SITES ARE REPLACED BY THE N-EPSILON AMINO GROUPS OF LYS |
| Chain | Residue |
| B | LYS680 |
| B | ASP744 |
| B | ASP786 |
| B | GLU716 |
| B | GLO960 |
| site_id | M2A |
| Number of Residues | 6 |
| Details | METAL BINDING SITE |
| Chain | Residue |
| A | ASP256 |
| A | OH1700 |
| A | MG401 |
| A | GLU216 |
| A | HIS219 |
| A | ASP254 |
| site_id | M2B |
| Number of Residues | 6 |
| Details | METAL BINDING SITE |
| Chain | Residue |
| B | MG901 |
| B | GLU716 |
| B | HIS719 |
| B | ASP754 |
| B | ASP756 |
| B | OH1800 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP54 | |
| A | LEU57 | |
| B | ASP554 | |
| B | LEU557 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PRO181 | |
| B | GLU720 | |
| B | LEU745 | |
| B | GLN755 | |
| B | LEU757 | |
| B | PHE787 | |
| A | VAL217 | |
| A | GLU220 | |
| A | LEU245 | |
| A | GLN255 | |
| A | LEU257 | |
| A | PHE287 | |
| B | PRO681 | |
| B | VAL717 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | ASP254 | |
| A | LYS182 | |
| A | HIS219 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | HIS719 | |
| B | ASP754 | |
| B | LYS682 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | ARG291 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | ARG791 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | LYS180 | |
| A | LYS182 | |
| A | ASP56 | |
| A | HIS53 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | HIS553 | |
| B | LYS680 | |
| B | LYS682 | |
| B | ASP556 | |
