1XLB
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 PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 399 |
Chain | Residue |
A | GLU180 |
A | GLU216 |
A | ASP244 |
A | ASP292 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 399 |
Chain | Residue |
B | GLU180 |
B | GLU216 |
B | ASP244 |
B | ASP292 |
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 | 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 |