3C48
Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure.
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 | 0016758 | molecular_function | hexosyltransferase 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 | 0016758 | molecular_function | hexosyltransferase 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 | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 419 |
| Chain | Residue |
| A | ARG125 |
| B | LEU291 |
| B | ARG294 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 419 |
| Chain | Residue |
| B | LEU257 |
| B | ARG258 |
| B | ARG287 |
| A | ARG2 |
| B | PHE249 |
| B | PRO253 |
| B | ASP254 |
| B | ARG255 |
| B | ASN256 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 420 |
| Chain | Residue |
| A | ARG97 |
| B | ARG125 |
| B | ARG215 |
| B | PRO220 |
| B | LEU221 |
| B | HIS222 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 420 |
| Chain | Residue |
| A | LYS78 |
| A | TYR110 |
| A | THR134 |
| A | LYS139 |
| A | ARG154 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 421 |
| Chain | Residue |
| B | ARG2 |
| B | THR102 |
| B | ASN206 |
| B | ARG212 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 421 |
| Chain | Residue |
| A | ARG50 |
| A | PRO51 |
| A | SER52 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 422 |
| Chain | Residue |
| B | ARG50 |
| B | PRO51 |
| B | SER52 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 423 |
| Chain | Residue |
| B | LYS78 |
| B | TYR110 |
| B | THR134 |
| B | LYS139 |
| B | ARG154 |
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 |
