6EBN
Crystal structure of Psilocybe cubensis noncanonical aromatic amino acid decarboxylase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 1101 |
| Chain | Residue |
| A | ASN61 |
| A | ALA62 |
| A | PHE63 |
| B | ASN691 |
| B | PHE693 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 1102 |
| Chain | Residue |
| A | ARG421 |
| A | GLU422 |
| A | HIS591 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 1103 |
| Chain | Residue |
| A | PRO934 |
| A | LEU935 |
| A | HIS936 |
| A | ASP937 |
| A | ILE938 |
| A | TYR925 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 1104 |
| Chain | Residue |
| A | HIS723 |
| A | THR724 |
| A | HIS738 |
| A | THR739 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 1105 |
| Chain | Residue |
| A | HIS430 |
| A | HOH1391 |
| B | HIS430 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue FMT A 1106 |
| Chain | Residue |
| A | HOH1304 |
| A | HOH1444 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue FMT A 1107 |
| Chain | Residue |
| A | ARG457 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue FMT A 1108 |
| Chain | Residue |
| A | ARG197 |
| A | ARG210 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue FMT A 1109 |
| Chain | Residue |
| A | LEU670 |
| A | GLY672 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 1110 |
| Chain | Residue |
| A | GLN629 |
| A | SER632 |
| A | GLU638 |
| A | ASP971 |
| A | HOH1451 |
| A | HOH1508 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 1111 |
| Chain | Residue |
| A | GLU824 |
| A | ASP825 |
| A | MET930 |
| A | HOH1443 |
| A | HOH1507 |
| A | HOH1588 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 1101 |
| Chain | Residue |
| A | ASN691 |
| B | ASN61 |
| B | ALA62 |
| B | HOH1508 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 1102 |
| Chain | Residue |
| B | ARG421 |
| B | GLU422 |
| B | HIS591 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 1103 |
| Chain | Residue |
| B | HIS723 |
| B | THR724 |
| B | HIS738 |
| B | THR739 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue FMT B 1104 |
| Chain | Residue |
| B | SER214 |
| B | LYS222 |
| B | HOH1387 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue FMT B 1105 |
| Chain | Residue |
| B | SER239 |
| B | ARG457 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue FMT B 1106 |
| Chain | Residue |
| B | ARG197 |
| B | ARG210 |
| B | HOH1534 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue FMT B 1107 |
| Chain | Residue |
| B | THR537 |
| B | ARG713 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue FMT B 1108 |
| Chain | Residue |
| B | VAL671 |
| B | GLY672 |
| B | HOH1231 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 1109 |
| Chain | Residue |
| B | GLN629 |
| B | SER632 |
| B | GLU638 |
| B | ASP971 |
| B | HOH1399 |
| B | HOH1425 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 1110 |
| Chain | Residue |
| B | GLU824 |
| B | ASP825 |
| B | MET930 |
| B | HOH1272 |
| B | HOH1521 |
| B | HOH1615 |
| site_id | AE4 |
| Number of Residues | 24 |
| Details | binding site for Di-peptide HIS B 442 and LLP B 443 |
| Chain | Residue |
| B | HOH1326 |
| A | SER489 |
| A | HOH1311 |
| A | HOH1343 |
| B | MET108 |
| B | SER173 |
| B | GLY174 |
| B | GLY175 |
| B | THR176 |
| B | ASN179 |
| B | HIS295 |
| B | THR352 |
| B | ASP382 |
| B | ASP440 |
| B | PRO441 |
| B | ALA444 |
| B | GLY445 |
| B | TYR446 |
| B | VAL447 |
| B | TYR449 |
| B | ALA451 |
| B | MET684 |
| B | HOH1236 |
| B | HOH1267 |
| site_id | AE5 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide LLP B 443 and ALA B 444 |
| Chain | Residue |
| A | SER489 |
| A | HOH1311 |
| B | MET108 |
| B | GLY174 |
| B | GLY175 |
| B | THR176 |
| B | ASN179 |
| B | HIS295 |
| B | THR352 |
| B | ASP382 |
| B | ASP440 |
| B | PRO441 |
| B | HIS442 |
| B | GLY445 |
| B | TYR446 |
| B | MET684 |
| B | HOH1236 |
| B | HOH1326 |
| B | HOH1404 |
Functional Information from PROSITE/UniProt
| site_id | PS00658 |
| Number of Residues | 7 |
| Details | FORK_HEAD_2 Fork head domain signature 2. WQNAVRH |
| Chain | Residue | Details |
| A | TRP995-HIS1001 |
