2Y7D
Crystal structure of the 3-keto-5-aminohexanoate cleavage enzyme (Kce) from Candidatus Cloacamonas acidaminovorans (orthorombic form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019475 | biological_process | L-lysine catabolic process to acetate |
| A | 0043720 | molecular_function | 3-keto-5-aminohexanoate cleavage activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019475 | biological_process | L-lysine catabolic process to acetate |
| B | 0043720 | molecular_function | 3-keto-5-aminohexanoate cleavage activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019475 | biological_process | L-lysine catabolic process to acetate |
| C | 0043720 | molecular_function | 3-keto-5-aminohexanoate cleavage activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019475 | biological_process | L-lysine catabolic process to acetate |
| D | 0043720 | molecular_function | 3-keto-5-aminohexanoate cleavage activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | HIS46 |
| A | HIS48 |
| A | GLU230 |
| A | HOH2247 |
| A | HOH2248 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | HOH2237 |
| B | HIS46 |
| B | HIS48 |
| B | GLU230 |
| B | HOH2236 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 301 |
| Chain | Residue |
| C | HIS46 |
| C | HIS48 |
| C | GLU230 |
| C | HOH2252 |
| C | HOH2253 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | HIS46 |
| D | HIS48 |
| D | GLU230 |
| D | HOH2235 |
| D | HOH2236 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 1276 |
| Chain | Residue |
| A | ALA13 |
| A | THR15 |
| A | ARG50 |
| A | GLY54 |
| A | PRO56 |
| A | HOH2064 |
| D | ASP52 |
| D | HOH2237 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1276 |
| Chain | Residue |
| B | ASP52 |
| B | HOH2238 |
| C | GLU14 |
| C | ARG50 |
| C | GLY54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21632536 |
| Chain | Residue | Details |
| A | GLU14 | |
| B | HIS48 | |
| B | SER82 | |
| B | THR106 | |
| B | ARG226 | |
| B | GLU230 | |
| C | GLU14 | |
| C | HIS46 | |
| C | HIS48 | |
| C | SER82 | |
| C | THR106 | |
| A | HIS46 | |
| C | ARG226 | |
| C | GLU230 | |
| D | GLU14 | |
| D | HIS46 | |
| D | HIS48 | |
| D | SER82 | |
| D | THR106 | |
| D | ARG226 | |
| D | GLU230 | |
| A | HIS48 | |
| A | SER82 | |
| A | THR106 | |
| A | ARG226 | |
| A | GLU230 | |
| B | GLU14 | |
| B | HIS46 |
