5XIN
PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES
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 SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | ASP55 | |
B | ASP55 | |
C | ASP55 | |
D | ASP55 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | LEU58 | |
B | LEU58 | |
C | LEU58 | |
D | LEU58 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | PRO182 | |
B | GLU221 | |
B | LEU246 | |
B | GLN256 | |
B | LEU258 | |
B | TYR293 | |
C | PRO182 | |
C | THR218 | |
C | GLU221 | |
C | LEU246 | |
C | GLN256 | |
A | THR218 | |
C | LEU258 | |
C | TYR293 | |
D | PRO182 | |
D | THR218 | |
D | GLU221 | |
D | LEU246 | |
D | GLN256 | |
D | LEU258 | |
D | TYR293 | |
A | GLU221 | |
A | LEU246 | |
A | GLN256 | |
A | LEU258 | |
A | TYR293 | |
B | PRO182 | |
B | THR218 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 2xis |
Chain | Residue | Details |
A | GLU181 | |
A | HIS54 | |
A | LYS183 | |
A | ASP57 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 2xis |
Chain | Residue | Details |
B | GLU181 | |
B | HIS54 | |
B | LYS183 | |
B | ASP57 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 2xis |
Chain | Residue | Details |
C | GLU181 | |
C | HIS54 | |
C | LYS183 | |
C | ASP57 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 2xis |
Chain | Residue | Details |
D | GLU181 | |
D | HIS54 | |
D | LYS183 | |
D | ASP57 |