1I8T
STRUCTURE OF UDP-GALACTOPYRANOSE MUTASE FROM E.COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 450 |
| Chain | Residue |
| A | VAL7 |
| A | ASN39 |
| A | TYR53 |
| A | ALA55 |
| A | HIS56 |
| A | ILE57 |
| A | ILE211 |
| A | ASP212 |
| A | PHE213 |
| A | THR230 |
| A | GLY231 |
| A | GLY8 |
| A | TYR310 |
| A | TYR311 |
| A | GLY339 |
| A | ARG340 |
| A | TYR346 |
| A | TYR347 |
| A | ASP348 |
| A | MET349 |
| A | HOH453 |
| A | HOH454 |
| A | GLY10 |
| A | HOH455 |
| A | HOH495 |
| A | HOH513 |
| A | LEU11 |
| A | PHE12 |
| A | GLU31 |
| A | LYS32 |
| A | ARG33 |
| A | GLY38 |
| site_id | AC2 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD B 451 |
| Chain | Residue |
| B | VAL7 |
| B | GLY8 |
| B | GLY10 |
| B | LEU11 |
| B | PHE12 |
| B | GLU31 |
| B | LYS32 |
| B | ARG33 |
| B | GLY38 |
| B | ASN39 |
| B | TYR53 |
| B | ALA55 |
| B | HIS56 |
| B | ILE57 |
| B | ILE211 |
| B | ASP212 |
| B | PHE213 |
| B | THR230 |
| B | GLY231 |
| B | PRO232 |
| B | TYR311 |
| B | GLY339 |
| B | ARG340 |
| B | TYR346 |
| B | TYR347 |
| B | ASP348 |
| B | MET349 |
| B | VAL352 |
| B | HOH452 |
| B | HOH457 |
| B | HOH462 |
| B | HOH463 |
| B | HOH470 |
| B | HOH548 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11573090","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details |
| Chain | Residue | Details |
| A | ASP348 | |
| A | ARG278 | |
| A | ARG170 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 368 |
| Chain | Residue | Details |
| A | ARG170 | electrostatic stabiliser |
| A | ARG174 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG247 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG278 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU298 | electrostatic stabiliser, hydrogen bond acceptor, steric role |
| A | TYR346 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | ASP348 | electrostatic stabiliser, steric role |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 368 |
| Chain | Residue | Details |
| B | ARG170 | electrostatic stabiliser |
| B | ARG174 | electrostatic stabiliser, hydrogen bond donor |
| B | ARG247 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG278 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU298 | electrostatic stabiliser, hydrogen bond acceptor, steric role |
| B | TYR346 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | ASP348 | electrostatic stabiliser, steric role |
