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 | 0016853 | molecular_function | isomerase activity |
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 | 0016853 | molecular_function | isomerase activity |
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: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | PHE12 | |
A | TYR346 | |
B | PHE12 | |
B | ASN80 | |
B | THR152 | |
B | TRP156 | |
B | TYR181 | |
B | ASN268 | |
B | ARG278 | |
B | TYR311 | |
B | ARG340 | |
A | ASN80 | |
B | TYR346 | |
A | THR152 | |
A | TRP156 | |
A | TYR181 | |
A | ASN268 | |
A | ARG278 | |
A | TYR311 | |
A | ARG340 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11573090 |
Chain | Residue | Details |
A | GLU31 | |
B | TYR347 | |
A | ASN39 | |
A | HIS56 | |
A | ASP212 | |
A | TYR347 | |
B | GLU31 | |
B | ASN39 | |
B | HIS56 | |
B | ASP212 |
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 |