4XIM
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 PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 395 |
| Chain | Residue |
| A | GLU181 |
| A | GLU217 |
| A | ASP245 |
| A | ASP292 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 396 |
| Chain | Residue |
| A | GLU217 |
| A | HIS220 |
| A | ASP255 |
| A | ASP257 |
| A | HOH530 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 395 |
| Chain | Residue |
| B | GLU181 |
| B | GLU217 |
| B | ASP245 |
| B | ASP292 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B 396 |
| Chain | Residue |
| B | GLU217 |
| B | HIS220 |
| B | ASP255 |
| B | ASP257 |
| B | HOH538 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO C 395 |
| Chain | Residue |
| C | GLU181 |
| C | GLU217 |
| C | ASP245 |
| C | ASP292 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO C 396 |
| Chain | Residue |
| C | GLU217 |
| C | HIS220 |
| C | ASP255 |
| C | ASP257 |
| C | HOH549 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO D 395 |
| Chain | Residue |
| D | GLU181 |
| D | GLU217 |
| D | ASP245 |
| D | ASP292 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO D 396 |
| Chain | Residue |
| D | GLU217 |
| D | HIS220 |
| D | ASP255 |
| D | ASP257 |
| D | HOH548 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | LYS183 | |
| A | HIS220 | |
| A | ASP255 |
| site_id | CSA10 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | GLU181 | |
| B | HIS54 | |
| B | LYS183 | |
| B | ASP57 |
| site_id | CSA11 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| C | GLU181 | |
| C | HIS54 | |
| C | LYS183 | |
| C | ASP57 |
| site_id | CSA12 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| D | GLU181 | |
| D | HIS54 | |
| D | LYS183 | |
| D | ASP57 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | LYS183 | |
| B | HIS220 | |
| B | ASP255 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| C | LYS183 | |
| C | HIS220 | |
| C | ASP255 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| D | LYS183 | |
| D | HIS220 | |
| D | ASP255 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | ARG297 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | ARG297 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| C | ARG297 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| D | ARG297 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | GLU181 | |
| A | HIS54 | |
| A | LYS183 | |
| A | ASP57 |
