1DIE
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 | 6 |
Details | BINDING SITE FOR RESIDUE MG A 398 |
Chain | Residue |
A | GLU216 |
A | HIS219 |
A | ASN246 |
A | ASP254 |
A | ASP256 |
A | HOH671 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 399 |
Chain | Residue |
A | ASP292 |
A | NOJ400 |
A | GLU180 |
A | GLU216 |
A | ASP244 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 398 |
Chain | Residue |
B | GLU216 |
B | HIS219 |
B | ASP254 |
B | ASP256 |
B | HOH688 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 399 |
Chain | Residue |
B | GLU180 |
B | GLU216 |
B | ASP244 |
B | ASP292 |
B | NOJ400 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE NOJ A 400 |
Chain | Residue |
A | HIS53 |
A | THR89 |
A | TRP136 |
A | GLU180 |
A | GLU216 |
A | HIS219 |
A | ASP244 |
A | ASP292 |
A | MG399 |
A | HOH482 |
A | HOH513 |
A | HOH514 |
A | HOH668 |
A | HOH671 |
B | PHE25 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NOJ B 400 |
Chain | Residue |
A | PHE25 |
B | HIS53 |
B | THR89 |
B | TRP136 |
B | GLU180 |
B | GLU216 |
B | HIS219 |
B | ASP244 |
B | ASP292 |
B | MG399 |
B | HOH671 |
B | HOH685 |
B | HOH686 |
B | HOH689 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:2319597 |
Chain | Residue | Details |
A | ASP54 | |
A | LEU57 | |
B | ASP54 | |
B | LEU57 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: |
Chain | Residue | Details |
A | PRO181 | |
B | GLU220 | |
B | LEU245 | |
B | GLN255 | |
B | LEU257 | |
B | TYR293 | |
A | THR217 | |
A | GLU220 | |
A | LEU245 | |
A | GLN255 | |
A | LEU257 | |
A | TYR293 | |
B | PRO181 | |
B | THR217 |
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 | ASP54 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | LEU257 | metal ligand |
A | TYR293 | activator, attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor |
A | LEU57 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | VAL88 | polar interaction, steric role |
A | PRO181 | metal ligand |
A | PRO183 | electrostatic stabiliser, hydrogen bond donor, proton donor |
A | THR217 | metal ligand |
A | GLU220 | metal ligand |
A | LEU245 | metal ligand |
A | GLN255 | metal ligand |
site_id | MCSA2 |
Number of Residues | 11 |
Details | M-CSA 308 |
Chain | Residue | Details |
B | ASP54 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | LEU257 | metal ligand |
B | TYR293 | activator, attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor |
B | LEU57 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | VAL88 | polar interaction, steric role |
B | PRO181 | metal ligand |
B | PRO183 | electrostatic stabiliser, hydrogen bond donor, proton donor |
B | THR217 | metal ligand |
B | GLU220 | metal ligand |
B | LEU245 | metal ligand |
B | GLN255 | metal ligand |