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 |
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 CO A 491 |
Chain | Residue |
A | GLU231 |
A | GLU267 |
A | ASP295 |
A | ASP338 |
A | HOH613 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CO A 492 |
Chain | Residue |
A | GLU267 |
A | HIS270 |
A | ASP306 |
A | ASP308 |
A | HOH613 |
A | HOH614 |
A | HOH615 |
A | HOH616 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CO A 493 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO D 491 |
Chain | Residue |
D | GLU231 |
D | GLU267 |
D | ASP295 |
D | ASP338 |
D | HOH618 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CO D 492 |
Chain | Residue |
D | GLU267 |
D | HIS270 |
D | ASP306 |
D | ASP308 |
D | HOH618 |
D | HOH619 |
D | HOH620 |
D | HOH621 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CO D 493 |
site_id | CO1 |
Number of Residues | 5 |
Details | CO BINDING SITE 1 OF MOLECULE A |
Chain | Residue |
A | GLU231 |
A | GLU267 |
A | ASP295 |
A | ASP338 |
A | HOH614 |
site_id | CO2 |
Number of Residues | 5 |
Details | CO BINDING SITE 2 OF MOLECULE A (HOH629 WAS ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS SITE). |
Chain | Residue |
A | HOH616 |
A | GLU267 |
A | HIS270 |
A | HOH614 |
A | HOH615 |
site_id | CO3 |
Number of Residues | 1 |
Details | CO BINDING SITE 3 OF MOLECULE A (SITE CO3 IS ON A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS: INTERPRETATION OF THE OBSERVED DENSITY PEAK AS A CO CATION WAS PRAGMATIC RATHER THAN RIGOROUS, AS THIS SITE IS CLEARLY NOT A FEATURE OF THE PROTEIN IN SOLUTION). |
site_id | CO4 |
Number of Residues | 5 |
Details | CO BINDING SITE 1 OF MOLECULE D |
Chain | Residue |
D | GLU231 |
D | GLU267 |
D | ASP295 |
D | ASP338 |
D | HOH619 |
site_id | CO5 |
Number of Residues | 5 |
Details | CO BINDING SITE 2 OF MOLECULE D (HOH629 WAS ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS SITE). |
Chain | Residue |
D | GLU267 |
D | HIS270 |
D | HOH619 |
D | HOH620 |
D | HOH621 |
site_id | CO6 |
Number of Residues | 1 |
Details | CO BINDING SITE 3 OF MOLECULE D (SITE CO3 IS ON A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS: INTERPRETATION OF THE OBSERVED DENSITY PEAK AS A CO CATION WAS PRAGMATIC RATHER THAN RIGOROUS, AS THIS SITE IS CLEARLY NOT A FEATURE OF THE PROTEIN IN SOLUTION). |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | HIS100 | |
D | HIS100 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | ASP103 | |
D | ASP103 | |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU231 | |
D | HIS270 | |
D | ASP295 | |
D | ASP306 | |
D | ASP308 | |
D | ASP338 | |
A | GLU267 | |
A | HIS270 | |
A | ASP295 | |
A | ASP306 | |
A | ASP308 | |
A | ASP338 | |
D | GLU231 | |
D | 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 |
D | ASP306 | |
D | HIS270 | |
D | LYS233 | |
site_id | CSA3 |
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 | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1de6 |
Chain | Residue | Details |
D | ASP103 | |
D | GLU231 | |
D | HIS100 | |
D | LYS233 | |