3RKS
Crystal Structure of the Manihot esculenta Hydroxynitrile Lyase (MeHNL) K176P mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016829 | molecular_function | lyase activity |
| A | 0047606 | molecular_function | hydroxynitrilase activity |
| A | 0052891 | molecular_function | aliphatic (S)-hydroxynitrile lyase activity |
| A | 0052892 | molecular_function | aromatic (S)-hydroxynitrile lyase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0047606 | molecular_function | hydroxynitrilase activity |
| B | 0052891 | molecular_function | aliphatic (S)-hydroxynitrile lyase activity |
| B | 0052892 | molecular_function | aromatic (S)-hydroxynitrile lyase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0047606 | molecular_function | hydroxynitrilase activity |
| C | 0052891 | molecular_function | aliphatic (S)-hydroxynitrile lyase activity |
| C | 0052892 | molecular_function | aromatic (S)-hydroxynitrile lyase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0047606 | molecular_function | hydroxynitrilase activity |
| D | 0052891 | molecular_function | aliphatic (S)-hydroxynitrile lyase activity |
| D | 0052892 | molecular_function | aromatic (S)-hydroxynitrile lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 259 |
| Chain | Residue |
| A | ILE43 |
| C | ARG175 |
| A | ASP44 |
| A | PRO45 |
| A | GLN47 |
| A | ARG175 |
| C | ILE43 |
| C | ASP44 |
| C | PRO45 |
| C | GLN47 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 259 |
| Chain | Residue |
| B | ILE43 |
| B | ASP44 |
| B | PRO45 |
| B | GLN47 |
| B | ARG175 |
| D | ILE43 |
| D | ASP44 |
| D | PRO45 |
| D | GLN47 |
| D | ARG175 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:11173464, ECO:0000305|PubMed:11316882 |
| Chain | Residue | Details |
| A | SER80 | |
| A | HIS236 | |
| B | SER80 | |
| B | HIS236 | |
| C | SER80 | |
| C | HIS236 | |
| D | SER80 | |
| D | HIS236 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11173464, ECO:0007744|PDB:1DWO |
| Chain | Residue | Details |
| A | THR11 | |
| D | THR11 | |
| D | SER80 | |
| D | CYS81 | |
| A | SER80 | |
| A | CYS81 | |
| B | THR11 | |
| B | SER80 | |
| B | CYS81 | |
| C | THR11 | |
| C | SER80 | |
| C | CYS81 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Increases basicity of active site His => ECO:0000305|PubMed:11316882 |
| Chain | Residue | Details |
| A | ASP208 | |
| B | ASP208 | |
| C | ASP208 | |
| D | ASP208 |
