1A0D
XYLOSE ISOMERASE FROM BACILLUS STEAROTHERMOPHILUS
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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0009045 | molecular_function | xylose isomerase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0042732 | biological_process | D-xylose metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0009045 | molecular_function | xylose isomerase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0042732 | biological_process | D-xylose metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 491 |
| Chain | Residue |
| A | GLU229 |
| A | GLU265 |
| A | ASP293 |
| A | ASP336 |
| A | HOH538 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 492 |
| Chain | Residue |
| A | GLU265 |
| A | HIS268 |
| A | ASP304 |
| A | ASP306 |
| A | HOH493 |
| A | HOH544 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 491 |
| Chain | Residue |
| B | GLU229 |
| B | GLU265 |
| B | ASP293 |
| B | ASP336 |
| B | HOH542 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 492 |
| Chain | Residue |
| B | GLU265 |
| B | HIS268 |
| B | ASP304 |
| B | ASP306 |
| B | HOH496 |
| B | HOH548 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 491 |
| Chain | Residue |
| C | GLU229 |
| C | GLU265 |
| C | ASP293 |
| C | ASP336 |
| C | HOH541 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 492 |
| Chain | Residue |
| C | GLU265 |
| C | HIS268 |
| C | ASP304 |
| C | ASP306 |
| C | HOH497 |
| C | HOH547 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 491 |
| Chain | Residue |
| D | GLU229 |
| D | GLU265 |
| D | ASP293 |
| D | ASP336 |
| D | HOH544 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 492 |
| Chain | Residue |
| D | GLU265 |
| D | HIS268 |
| D | ASP304 |
| D | ASP306 |
| D | HOH499 |
| D | HOH550 |
| site_id | MN1 |
| Number of Residues | 5 |
| Details | MN BINDING SITE 1 OF MOLECULE A |
| Chain | Residue |
| A | GLU229 |
| A | GLU265 |
| A | ASP293 |
| A | ASP336 |
| A | HOH538 |
| site_id | MN2 |
| Number of Residues | 5 |
| Details | MN BINDING SITE 2 OF MOLECULE A |
| Chain | Residue |
| A | HOH545 |
| A | GLU265 |
| A | ASP304 |
| A | ASP306 |
| A | HOH493 |
| site_id | MN3 |
| Number of Residues | 5 |
| Details | MN BINDING SITE 1 OF MOLECULE B |
| Chain | Residue |
| B | GLU229 |
| B | GLU265 |
| B | ASP293 |
| B | ASP336 |
| B | HOH542 |
| site_id | MN4 |
| Number of Residues | 5 |
| Details | MN BINDING SITE 2 OF MOLECULE B |
| Chain | Residue |
| B | GLU265 |
| B | ASP304 |
| B | ASP306 |
| B | HOH496 |
| B | HOH549 |
| site_id | MN5 |
| Number of Residues | 5 |
| Details | MN BINDING SITE 1 OF MOLECULE C |
| Chain | Residue |
| C | GLU229 |
| C | GLU265 |
| C | ASP293 |
| C | ASP336 |
| C | HOH541 |
| site_id | MN6 |
| Number of Residues | 5 |
| Details | MN BINDING SITE 2 OF MOLECULE C |
| Chain | Residue |
| C | GLU265 |
| C | ASP304 |
| C | ASP306 |
| C | HOH497 |
| C | HOH548 |
| site_id | MN7 |
| Number of Residues | 5 |
| Details | MN BINDING SITE 1 OF MOLECULE D |
| Chain | Residue |
| D | GLU229 |
| D | GLU265 |
| D | ASP293 |
| D | ASP336 |
| D | HOH544 |
| site_id | MN8 |
| Number of Residues | 5 |
| Details | MN BINDING SITE 2 OF MOLECULE D |
| Chain | Residue |
| D | GLU265 |
| D | ASP304 |
| D | ASP306 |
| D | HOH499 |
| D | HOH551 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | HIS98 | |
| B | HIS98 | |
| C | HIS98 | |
| D | HIS98 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP101 | |
| B | ASP101 | |
| C | ASP101 | |
| D | ASP101 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU229 | |
| B | ASP304 | |
| B | ASP306 | |
| B | ASP336 | |
| C | GLU229 | |
| C | GLU265 | |
| C | ASP293 | |
| C | ASP304 | |
| C | ASP306 | |
| C | ASP336 | |
| D | GLU229 | |
| A | GLU265 | |
| D | GLU265 | |
| D | ASP293 | |
| D | ASP304 | |
| D | ASP306 | |
| D | ASP336 | |
| A | ASP293 | |
| A | ASP304 | |
| A | ASP306 | |
| A | ASP336 | |
| B | GLU229 | |
| B | GLU265 | |
| B | ASP293 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | ASP304 | |
| A | LYS231 | |
| A | HIS268 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | ASP304 | |
| B | LYS231 | |
| B | HIS268 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| C | ASP304 | |
| C | LYS231 | |
| C | HIS268 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| D | ASP304 | |
| D | LYS231 | |
| D | HIS268 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | HIS98 | |
| A | LYS231 | |
| A | GLU229 | |
| A | ASP101 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | HIS98 | |
| B | LYS231 | |
| B | GLU229 | |
| B | ASP101 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| C | HIS98 | |
| C | LYS231 | |
| C | GLU229 | |
| C | ASP101 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| D | HIS98 | |
| D | LYS231 | |
| D | GLU229 | |
| D | ASP101 |
