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 | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 400 |
| Chain | Residue |
| A | GLU180 |
| A | GLU216 |
| A | ASP244 |
| A | ASP286 |
| A | HYA960 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | GLU216 |
| A | HIS219 |
| A | ASP256 |
| A | HYA960 |
| A | HOH1700 |
| A | HOH1701 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 400 |
| Chain | Residue |
| B | GLU180 |
| B | GLU216 |
| B | ASP244 |
| B | ASP286 |
| B | MG401 |
| B | HYA970 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | GLU216 |
| B | HIS219 |
| B | MG400 |
| B | HYA970 |
| B | HOH1800 |
| B | HOH1801 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HYA A 960 |
| Chain | Residue |
| A | TRP15 |
| A | HIS53 |
| A | PHE93 |
| A | TRP136 |
| A | GLU180 |
| A | LYS182 |
| A | GLU216 |
| A | HIS219 |
| A | ASP244 |
| A | ASP286 |
| A | MG400 |
| A | MG401 |
| A | HOH1166 |
| A | HOH1170 |
| A | HOH1338 |
| A | HOH1700 |
| B | PHE25 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HYA B 970 |
| Chain | Residue |
| A | PHE25 |
| B | TRP15 |
| B | HIS53 |
| B | PHE93 |
| B | TRP136 |
| B | GLU180 |
| B | LYS182 |
| B | HIS219 |
| B | ASP244 |
| B | ASP286 |
| B | MG400 |
| B | MG401 |
| B | HOH1279 |
| B | HOH1281 |
| B | HOH1539 |
| B | HOH1800 |
| site_id | HYA |
| Number of Residues | 3 |
| Details | INHIBITOR, D-THREONOHYDROXAMIC ACID BINDING SITE IN MONOMER A |
| Chain | Residue |
| A | HYA960 |
| A | LYS182 |
| A | HIS53 |
| site_id | HYB |
| Number of Residues | 3 |
| Details | INHIBITOR, D-THREONOHYDROXAMIC ACID BINDING SITE IN MONOMER B |
| Chain | Residue |
| B | HYA970 |
| B | LYS182 |
| B | HIS53 |
| site_id | M1A |
| Number of Residues | 6 |
| Details | METAL BINDING SITE 1 IN MONOMER A ACTIVE SITE |
| Chain | Residue |
| A | MG400 |
| A | GLU180 |
| A | ASP244 |
| A | ASP286 |
| A | GLU216 |
| A | HYA960 |
| site_id | M1B |
| Number of Residues | 6 |
| Details | METAL BINDING SITE 1 IN MONOMER B ACTIVE SITE |
| Chain | Residue |
| B | MG400 |
| B | GLU180 |
| B | ASP244 |
| B | ASP286 |
| B | GLU216 |
| B | HYA970 |
| site_id | M2A |
| Number of Residues | 6 |
| Details | METAL BINDING SITE 2 IN MONOMER A ACTIVE SITE |
| Chain | Residue |
| A | HYA960 |
| A | HOH1700 |
| A | HOH1701 |
| A | MG401 |
| A | GLU216 |
| A | HIS219 |
| site_id | M2B |
| Number of Residues | 6 |
| Details | METAL BINDING SITE 2 IN MONOMER B ACTIVE SITE |
| Chain | Residue |
| B | MG401 |
| B | GLU216 |
| B | HIS219 |
| B | HYA970 |
| B | HOH1800 |
| B | HOH1801 |
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 | ASP54 | |
| B | LEU57 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PRO181 | |
| B | GLU220 | |
| B | LEU245 | |
| B | GLN255 | |
| B | LEU257 | |
| B | PHE287 | |
| A | VAL217 | |
| A | GLU220 | |
| A | LEU245 | |
| A | GLN255 | |
| A | LEU257 | |
| A | PHE287 | |
| B | PRO181 | |
| B | VAL217 | |
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 | ASP254 | |
| B | LYS182 | |
| B | HIS219 | |
| 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 | ARG291 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | GLU180 | |
| 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 | GLU180 | |
| B | LYS182 | |
| B | ASP56 | |
| B | HIS53 | |
