5ZHB
Structure of Cellobiose 2-Epimerase from Bacillus thermoamylovorans B4167
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| A | 0006051 | biological_process | N-acetylmannosamine metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030414 | molecular_function | peptidase inhibitor activity |
| A | 0047736 | molecular_function | cellobiose epimerase activity |
| A | 0050121 | molecular_function | N-acylglucosamine 2-epimerase activity |
| A | 0061593 | molecular_function | sulfoquinovose isomerase activity |
| A | 0061720 | biological_process | 6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| B | 0006051 | biological_process | N-acetylmannosamine metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
| B | 0047736 | molecular_function | cellobiose epimerase activity |
| B | 0050121 | molecular_function | N-acylglucosamine 2-epimerase activity |
| B | 0061593 | molecular_function | sulfoquinovose isomerase activity |
| B | 0061720 | biological_process | 6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | GLY48 |
| A | GLY49 |
| A | ILE50 |
| A | ALA51 |
| A | TRP96 |
| A | PRO370 |
| A | TRP371 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | GLY349 |
| B | GLU348 |
| A | PHE19 |
| A | LYS22 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | LYS163 |
| B | TYR342 |
| B | ALA358 |
| B | GLY360 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | TYR119 |
| A | GLU191 |
| A | ARG198 |
| A | ASP257 |
| A | EDO405 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | TRP57 |
| A | ARG64 |
| A | ARG379 |
| A | LEU382 |
| A | GLU383 |
| A | GLU386 |
| A | EDO404 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | HIS40 |
| A | VAL41 |
| B | SER346 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ARG54 |
| A | TRP371 |
| A | HIS376 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 401 |
| Chain | Residue |
| B | TRP57 |
| B | ARG64 |
| B | ARG379 |
| B | LEU382 |
| B | GLU383 |
| B | GLU386 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | TYR112 |
| B | ASN184 |
| B | HIS188 |
| B | HIS247 |
| B | GLU250 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | GLY30 |
| B | TYR31 |
| B | TYR32 |
| B | LYS47 |
| B | THR52 |
| B | GLN55 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| A | GLU348 |
| B | GLY349 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| A | SER105 |
| A | ASP106 |
| A | ASP107 |
