2X2J
Crystal structure of the Gracilariopsis lemaneiformis alpha- 1,4-glucan lyase with deoxynojirimycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0047457 | molecular_function | exo-(1,4)-alpha-D-glucan lyase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0047457 | molecular_function | exo-(1,4)-alpha-D-glucan lyase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0047457 | molecular_function | exo-(1,4)-alpha-D-glucan lyase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0016829 | molecular_function | lyase activity |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0047457 | molecular_function | exo-(1,4)-alpha-D-glucan lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NOJ A 1050 |
| Chain | Residue |
| A | PHE373 |
| A | PHE698 |
| A | HIS731 |
| A | HOH3301 |
| A | HOH3442 |
| A | ASP412 |
| A | ASN459 |
| A | TYR513 |
| A | TRP551 |
| A | ASP553 |
| A | ARG649 |
| A | TRP662 |
| A | ASP665 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NOJ B 1050 |
| Chain | Residue |
| B | PHE373 |
| B | ASP412 |
| B | ASN459 |
| B | TYR513 |
| B | TRP551 |
| B | ASP553 |
| B | ARG649 |
| B | TRP662 |
| B | ASP665 |
| B | PHE698 |
| B | HIS731 |
| B | HOH3192 |
| B | HOH3251 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NOJ C 1050 |
| Chain | Residue |
| C | PHE373 |
| C | ASP412 |
| C | ASN459 |
| C | TYR513 |
| C | TRP551 |
| C | ASP553 |
| C | MET554 |
| C | ARG649 |
| C | TRP662 |
| C | ASP665 |
| C | PHE698 |
| C | HIS731 |
| C | HOH3235 |
| C | HOH3459 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NOJ D 1050 |
| Chain | Residue |
| D | PHE373 |
| D | ASP412 |
| D | ASN459 |
| D | TYR513 |
| D | ASP553 |
| D | MET554 |
| D | ARG649 |
| D | TRP662 |
| D | ASP665 |
| D | PHE698 |
| D | HIS731 |
| D | HOH3165 |
| D | HOH3217 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 2039 |
| Chain | Residue |
| C | THR24 |
| C | VAL28 |
| C | GLY32 |
| C | PHE33 |
| C | GLN318 |
| C | HOH3460 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 2040 |
| Chain | Residue |
| C | LYS363 |
| C | ARG885 |
| C | TYR898 |
| C | THR899 |
| C | ASP900 |
| C | GLY925 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 2039 |
| Chain | Residue |
| A | MET792 |
| A | ASN794 |
| A | ASP813 |
| A | TYR815 |
| A | ARG877 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 2040 |
| Chain | Residue |
| A | ASP958 |
| A | CYS959 |
| A | TYR960 |
| A | GLU961 |
| A | HOH3412 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 2041 |
| Chain | Residue |
| A | LYS363 |
| A | TYR773 |
| A | ARG885 |
| A | ASP900 |
| A | ASP923 |
| A | ASP924 |
| A | GLY925 |
| A | HOH3330 |
| A | HOH3443 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 2042 |
| Chain | Residue |
| A | THR668 |
| A | THR669 |
| A | SER670 |
| A | TYR701 |
| A | THR711 |
| A | GLU825 |
| A | HOH3350 |
| A | HOH3444 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 2043 |
| Chain | Residue |
| A | TRP824 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 2042 |
| Chain | Residue |
| C | MET792 |
| C | ASN794 |
| C | ASP813 |
| C | TYR815 |
| C | ARG877 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 2039 |
| Chain | Residue |
| B | ASN794 |
| B | ASP813 |
| B | TYR815 |
| B | ARG877 |
| B | TYR793 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 2039 |
| Chain | Residue |
| D | TYR793 |
| D | ASN794 |
| D | TYR815 |
| D | ARG877 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 2044 |
| Chain | Residue |
| A | THR555 |
| A | ARG649 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 2040 |
| Chain | Residue |
| B | THR555 |
| B | VAL556 |
| B | ARG649 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 2043 |
| Chain | Residue |
| C | TYR266 |
| C | THR555 |
| C | ARG649 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 2040 |
| Chain | Residue |
| D | THR555 |
| D | ARG649 |
