6EEI
Crystal structure of Arabidopsis thaliana phenylacetaldehyde synthase in complex with L-phenylalanine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006559 | biological_process | L-phenylalanine catabolic process |
A | 0009611 | biological_process | response to wounding |
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 | 0003824 | molecular_function | catalytic activity |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0006559 | biological_process | L-phenylalanine catabolic process |
B | 0009611 | biological_process | response to wounding |
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 | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32371491, ECO:0007744|PDB:6EEI |
Chain | Residue | Details |
A | PRO92 | |
A | HIS193 | |
A | HIS308 | |
A | PHE338 | |
B | PRO92 | |
B | HIS193 | |
B | HIS308 | |
B | PHE338 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:32371491 |
Chain | Residue | Details |
A | LLP309 | |
B | LLP309 |