1A0C
XYLOSE ISOMERASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES
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 | 6 |
| Details | BINDING SITE FOR RESIDUE CO A 491 |
| Chain | Residue |
| A | GLU231 |
| A | GLU267 |
| A | ASP295 |
| A | ASP338 |
| A | HOH494 |
| A | HOH495 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 492 |
| Chain | Residue |
| A | GLU267 |
| A | HIS270 |
| A | ASP306 |
| A | ASP308 |
| A | HOH493 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B 491 |
| Chain | Residue |
| B | GLU231 |
| B | GLU267 |
| B | ASP295 |
| B | ASP338 |
| B | HOH527 |
| B | HOH528 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B 492 |
| Chain | Residue |
| B | GLU267 |
| B | HIS270 |
| B | ASP306 |
| B | ASP308 |
| B | HOH526 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO C 491 |
| Chain | Residue |
| C | GLU231 |
| C | GLU267 |
| C | ASP295 |
| C | ASP338 |
| C | HOH525 |
| C | HOH526 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO C 492 |
| Chain | Residue |
| C | GLU267 |
| C | HIS270 |
| C | ASP306 |
| C | ASP308 |
| C | HOH524 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO D 491 |
| Chain | Residue |
| D | GLU231 |
| D | GLU267 |
| D | ASP295 |
| D | ASP338 |
| D | HOH558 |
| D | HOH559 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO D 492 |
| Chain | Residue |
| D | GLU267 |
| D | HIS270 |
| D | ASP306 |
| D | ASP308 |
| D | HOH557 |
| site_id | CO1 |
| Number of Residues | 6 |
| Details | CO BINDING SITE 1 OF MOLECULE A |
| Chain | Residue |
| A | GLU231 |
| A | GLU267 |
| A | ASP295 |
| A | ASP338 |
| A | HOH494 |
| A | HOH495 |
| site_id | CO2 |
| Number of Residues | 5 |
| Details | CO BINDING SITE 2 OF MOLECULE A |
| Chain | Residue |
| A | ASP308 |
| A | HOH493 |
| A | GLU267 |
| A | HIS270 |
| A | ASP306 |
| site_id | CO3 |
| Number of Residues | 6 |
| Details | CO BINDING SITE 1 OF MOLECULE B |
| Chain | Residue |
| B | GLU231 |
| B | GLU267 |
| B | ASP295 |
| B | ASP338 |
| B | HOH527 |
| B | HOH528 |
| site_id | CO4 |
| Number of Residues | 5 |
| Details | CO BINDING SITE 2 OF MOLECULE B |
| Chain | Residue |
| B | GLU267 |
| B | HIS270 |
| B | ASP306 |
| B | ASP308 |
| B | HOH526 |
| site_id | CO5 |
| Number of Residues | 6 |
| Details | CO BINDING SITE 1 OF MOLECULE C |
| Chain | Residue |
| C | GLU231 |
| C | GLU267 |
| C | ASP295 |
| C | ASP338 |
| C | HOH525 |
| C | HOH526 |
| site_id | CO6 |
| Number of Residues | 5 |
| Details | CO BINDING SITE 2 OF MOLECULE C |
| Chain | Residue |
| C | GLU267 |
| C | HIS270 |
| C | ASP306 |
| C | ASP308 |
| C | HOH524 |
| site_id | CO7 |
| Number of Residues | 6 |
| Details | CO BINDING SITE 1 OF MOLECULE D |
| Chain | Residue |
| D | GLU231 |
| D | GLU267 |
| D | ASP295 |
| D | ASP338 |
| D | HOH558 |
| D | HOH559 |
| site_id | CO8 |
| Number of Residues | 5 |
| Details | CO BINDING SITE 2 OF MOLECULE D |
| Chain | Residue |
| D | GLU267 |
| D | HIS270 |
| D | ASP306 |
| D | ASP308 |
| D | HOH557 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | HIS100 | |
| B | HIS100 | |
| C | HIS100 | |
| D | HIS100 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP103 | |
| B | ASP103 | |
| C | ASP103 | |
| D | ASP103 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU231 | |
| B | HIS270 | |
| B | ASP295 | |
| B | ASP306 | |
| B | ASP308 | |
| B | ASP338 | |
| C | GLU231 | |
| C | GLU267 | |
| C | HIS270 | |
| C | ASP295 | |
| C | ASP306 | |
| A | GLU267 | |
| C | ASP308 | |
| C | ASP338 | |
| D | GLU231 | |
| D | GLU267 | |
| D | HIS270 | |
| D | ASP295 | |
| D | ASP306 | |
| D | ASP308 | |
| D | ASP338 | |
| A | HIS270 | |
| A | ASP295 | |
| A | ASP306 | |
| A | ASP308 | |
| A | ASP338 | |
| B | GLU231 | |
| B | GLU267 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | ASP306 | |
| A | HIS270 | |
| A | LYS233 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | ASP306 | |
| B | HIS270 | |
| B | LYS233 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| C | ASP306 | |
| C | HIS270 | |
| C | LYS233 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| D | ASP306 | |
| D | HIS270 | |
| D | LYS233 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | ASP103 | |
| A | GLU231 | |
| A | HIS100 | |
| A | LYS233 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | ASP103 | |
| B | GLU231 | |
| B | HIS100 | |
| B | LYS233 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| C | ASP103 | |
| C | GLU231 | |
| C | HIS100 | |
| C | LYS233 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| D | ASP103 | |
| D | GLU231 | |
| D | HIS100 | |
| D | LYS233 |
