1DID
OBSERVATIONS OF REACTION INTERMEDIATES AND THE MECHANISM OF ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE
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 | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DIG A 400 |
| Chain | Residue |
| A | TRP15 |
| A | ASP292 |
| A | MN399 |
| A | HOH498 |
| A | HOH499 |
| A | HIS53 |
| A | MET87 |
| A | VAL134 |
| A | TRP136 |
| A | GLU180 |
| A | GLU216 |
| A | ASP244 |
| A | HIS290 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DIG B 400 |
| Chain | Residue |
| B | TRP15 |
| B | HIS53 |
| B | MET87 |
| B | VAL134 |
| B | TRP136 |
| B | GLU180 |
| B | ASN214 |
| B | GLU216 |
| B | ASP244 |
| B | HIS290 |
| B | ASP292 |
| B | MN399 |
| B | HOH519 |
| B | HOH520 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 398 |
| Chain | Residue |
| A | GLU216 |
| A | HIS219 |
| A | ASP254 |
| A | ASP256 |
| A | HOH498 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 399 |
| Chain | Residue |
| A | GLU180 |
| A | GLU216 |
| A | ASP244 |
| A | ASP292 |
| A | DIG400 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 398 |
| Chain | Residue |
| B | GLU216 |
| B | HIS219 |
| B | ASP254 |
| B | ASP256 |
| B | HOH519 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 399 |
| Chain | Residue |
| B | GLU180 |
| B | GLU216 |
| B | ASP244 |
| B | ASP292 |
| B | DIG400 |
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 |
