1XLC
MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT
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 SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"2319597","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| 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 | ASP254 | |
| A | LYS182 | |
| A | HIS219 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | ASP254 | |
| B | LYS182 | |
| B | HIS219 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | ARG297 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | ARG297 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | GLU180 | |
| 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 | GLU180 | |
| B | LYS182 | |
| B | ASP56 | |
| B | HIS53 |
| site_id | MCSA1 |
| Number of Residues | 11 |
| Details | M-CSA 308 |
| Chain | Residue | Details |
| A | HIS53 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP256 | metal ligand |
| A | ASP292 | activator, attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor |
| A | ASP56 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | MET87 | polar interaction, steric role |
| A | GLU180 | metal ligand |
| A | LYS182 | electrostatic stabiliser, hydrogen bond donor, proton donor |
| A | GLU216 | metal ligand |
| A | HIS219 | metal ligand |
| A | ASP244 | metal ligand |
| A | ASP254 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 11 |
| Details | M-CSA 308 |
| Chain | Residue | Details |
| B | HIS53 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP256 | metal ligand |
| B | ASP292 | activator, attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor |
| B | ASP56 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | MET87 | polar interaction, steric role |
| B | GLU180 | metal ligand |
| B | LYS182 | electrostatic stabiliser, hydrogen bond donor, proton donor |
| B | GLU216 | metal ligand |
| B | HIS219 | metal ligand |
| B | ASP244 | metal ligand |
| B | ASP254 | metal ligand |
