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 | |