7V8T
Crystal structure of class II pyruvate aldolase from Pseudomonas aeruginosa.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0010124 | biological_process | phenylacetate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0010124 | biological_process | phenylacetate catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016832 | molecular_function | aldehyde-lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0010124 | biological_process | phenylacetate catabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016832 | molecular_function | aldehyde-lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0010124 | biological_process | phenylacetate catabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016832 | molecular_function | aldehyde-lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0010124 | biological_process | phenylacetate catabolic process |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016832 | molecular_function | aldehyde-lyase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0010124 | biological_process | phenylacetate catabolic process |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016832 | molecular_function | aldehyde-lyase activity |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q47098 |
| Chain | Residue | Details |
| A | HIS48 | |
| B | HIS48 | |
| C | HIS48 | |
| D | HIS48 | |
| E | HIS48 | |
| F | HIS48 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q47098 |
| Chain | Residue | Details |
| A | GLU152 | |
| E | ASP178 | |
| F | GLU152 | |
| F | ASP178 | |
| A | ASP178 | |
| B | GLU152 | |
| B | ASP178 | |
| C | GLU152 | |
| C | ASP178 | |
| D | GLU152 | |
| D | ASP178 | |
| E | GLU152 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:Q47098 |
| Chain | Residue | Details |
| A | ARG73 | |
| B | ARG73 | |
| C | ARG73 | |
| D | ARG73 | |
| E | ARG73 | |
| F | ARG73 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | SITE: Increases basicity of active site His => ECO:0000250|UniProtKB:Q47098 |
| Chain | Residue | Details |
| A | ASP87 | |
| B | ASP87 | |
| C | ASP87 | |
| D | ASP87 | |
| E | ASP87 | |
| F | ASP87 |
