6EEI
Crystal structure of Arabidopsis thaliana phenylacetaldehyde synthase in complex with L-phenylalanine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006559 | biological_process | L-phenylalanine catabolic process |
| A | 0009611 | biological_process | response to wounding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0106425 | molecular_function | 3,4-dihydroxyphenylacetaldehyde synthase activity |
| A | 1990055 | molecular_function | phenylacetaldehyde synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006559 | biological_process | L-phenylalanine catabolic process |
| B | 0009611 | biological_process | response to wounding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0106425 | molecular_function | 3,4-dihydroxyphenylacetaldehyde synthase activity |
| B | 1990055 | molecular_function | phenylacetaldehyde synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | GLU378 |
| A | LYS381 |
| A | ARG385 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PHE A 502 |
| Chain | Residue |
| A | TYR90 |
| A | TYR91 |
| A | HIS193 |
| A | LLP309 |
| B | PHE114 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| B | GLU378 |
| B | LYS381 |
| B | ARG385 |
| B | PRO288 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PHE B 502 |
| Chain | Residue |
| A | PHE114 |
| B | TYR90 |
| B | TYR91 |
| B | THR252 |
| B | LLP309 |
| B | HOH603 |
Functional Information from PROSITE/UniProt
| site_id | PS00392 |
| Number of Residues | 22 |
| Details | DDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SFnMnahKWFlTnFDCslLWvK |
| Chain | Residue | Details |
| A | SER302-LYS323 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32371491","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EEI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"32371491","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
