3C4Q
Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008375 | molecular_function | acetylglucosaminyltransferase activity |
| A | 0010125 | biological_process | mycothiol biosynthetic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0102710 | molecular_function | D-inositol-3-phosphate glycosyltransferase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008375 | molecular_function | acetylglucosaminyltransferase activity |
| B | 0010125 | biological_process | mycothiol biosynthetic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0102710 | molecular_function | D-inositol-3-phosphate glycosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 602 |
| Chain | Residue |
| A | TYR303 |
| A | ARG304 |
| A | ALA306 |
| A | THR330 |
| A | HOH606 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 602 |
| Chain | Residue |
| B | HOH606 |
| B | HOH624 |
| B | TYR303 |
| B | ARG304 |
| B | ALA306 |
| B | THR330 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | LYS78 |
| A | TYR110 |
| A | THR134 |
| A | ARG154 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 603 |
| Chain | Residue |
| B | TYR110 |
| B | THR134 |
| B | ARG154 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE UDP A 600 |
| Chain | Residue |
| A | GLN15 |
| A | PRO16 |
| A | GLY17 |
| A | GLY23 |
| A | TYR202 |
| A | ARG231 |
| A | LYS236 |
| A | CYS262 |
| A | PRO293 |
| A | ARG294 |
| A | GLU316 |
| A | LEU320 |
| A | GLU324 |
| A | HOH613 |
| A | HOH616 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UDP B 600 |
| Chain | Residue |
| B | GLN15 |
| B | PRO16 |
| B | GLY17 |
| B | GLY22 |
| B | GLY23 |
| B | TYR202 |
| B | ARG231 |
| B | LYS236 |
| B | CYS262 |
| B | PRO293 |
| B | ARG294 |
| B | LEU299 |
| B | GLU316 |
| B | GLY319 |
| B | LEU320 |
| B | GLU324 |
| B | HOH615 |
| B | HOH630 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS9 | |
| A | LYS236 | |
| A | ARG294 | |
| A | TYR303 | |
| A | ARG304 | |
| A | ALA306 | |
| A | GLU316 | |
| A | GLU324 | |
| A | THR330 | |
| B | HIS9 | |
| B | GLN15 | |
| A | GLN15 | |
| B | ASP20 | |
| B | GLY23 | |
| B | LYS78 | |
| B | TYR110 | |
| B | THR134 | |
| B | ARG154 | |
| B | ARG231 | |
| B | LYS236 | |
| B | ARG294 | |
| B | TYR303 | |
| A | ASP20 | |
| B | ARG304 | |
| B | ALA306 | |
| B | GLU316 | |
| B | GLU324 | |
| B | THR330 | |
| A | GLY23 | |
| A | LYS78 | |
| A | TYR110 | |
| A | THR134 | |
| A | ARG154 | |
| A | ARG231 |
