6EEW
Crystal structure of Catharanthus roseus tryptophan decarboxylase in complex with L-tryptophan
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| 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 | 0036467 | molecular_function | 5-hydroxy-L-tryptophan decarboxylase activity |
| A | 0036469 | molecular_function | L-tryptophan decarboxylase activity |
| B | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| 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 | 0036467 | molecular_function | 5-hydroxy-L-tryptophan decarboxylase activity |
| B | 0036469 | molecular_function | L-tryptophan decarboxylase activity |
| C | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0036467 | molecular_function | 5-hydroxy-L-tryptophan decarboxylase activity |
| C | 0036469 | molecular_function | L-tryptophan decarboxylase activity |
| D | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0036467 | molecular_function | 5-hydroxy-L-tryptophan decarboxylase activity |
| D | 0036469 | molecular_function | L-tryptophan decarboxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue TRP A 601 |
| Chain | Residue |
| A | PHE100 |
| A | PHE101 |
| A | THR262 |
| A | LLP319 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CA A 602 |
| Chain | Residue |
| A | ASP397 |
| A | HOH716 |
| A | HOH728 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue TRP B 601 |
| Chain | Residue |
| B | PHE101 |
| B | HIS318 |
| B | LLP319 |
| A | PHE124 |
| B | TRP92 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 602 |
| Chain | Residue |
| B | ASP397 |
| B | HOH709 |
| B | HOH745 |
| B | HOH749 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue TRP C 601 |
| Chain | Residue |
| C | TRP92 |
| C | PHE101 |
| C | HIS203 |
| C | THR262 |
| C | HIS318 |
| C | LLP319 |
| D | THR369 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CA C 602 |
| Chain | Residue |
| C | ASP397 |
| C | HOH715 |
| C | HOH738 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue TRP D 601 |
| Chain | Residue |
| C | VAL122 |
| C | PHE124 |
| C | THR369 |
| D | HIS318 |
| D | LLP319 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue CA D 602 |
| Chain | Residue |
| D | ASP397 |
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. SLsLsphKWLlAyLDCtcLWvK |
| Chain | Residue | Details |
| A | SER312-LYS333 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32371491","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EEW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"32371491","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
