4OBV
Ruminococcus gnavus tryptophan decarboxylase RUMGNA_01526 (alpha-FMT)
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 | 0006568 | biological_process | tryptophan 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 | 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 | 0006568 | biological_process | tryptophan 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 | 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 | 0006568 | biological_process | tryptophan 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 | 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 | 0006568 | biological_process | tryptophan 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 | 0036469 | molecular_function | L-tryptophan decarboxylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 2SU D 501 |
Chain | Residue |
B | ILE19 |
D | LYS40 |
D | PRO102 |
D | ALA103 |
D | SER104 |
D | SER105 |
D | PHE309 |
D | PRO462 |
D | GLU463 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 3SO D 502 |
Chain | Residue |
B | HIS120 |
B | LEU336 |
B | TRP349 |
B | THR356 |
D | VAL99 |
D | GLY159 |
D | SER160 |
D | HIS192 |
D | SER194 |
D | THR249 |
D | ASP274 |
D | ALA276 |
D | ASP303 |
D | HIS305 |
D | LYS306 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 2SU C 501 |
Chain | Residue |
A | ILE19 |
C | PRO102 |
C | ALA103 |
C | SER104 |
C | SER105 |
C | PHE309 |
C | PRO462 |
C | GLU463 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 2SU B 501 |
Chain | Residue |
B | PRO102 |
B | ALA103 |
B | SER105 |
B | PHE309 |
B | PRO462 |
B | GLU463 |
D | ILE19 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 3SO B 502 |
Chain | Residue |
B | PHE98 |
B | VAL99 |
B | GLY159 |
B | SER160 |
B | HIS192 |
B | SER194 |
B | THR249 |
B | ASP274 |
B | ALA276 |
B | ASP303 |
B | LYS306 |
D | HIS120 |
D | TRP349 |
D | THR356 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 3SO A 501 |
Chain | Residue |
A | HIS120 |
A | TRP349 |
A | THR356 |
C | PHE98 |
C | VAL99 |
C | GLY159 |
C | SER160 |
C | HIS192 |
C | SER194 |
C | THR249 |
C | ASP274 |
C | ALA276 |
C | ASP303 |
C | LYS306 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 2SU A 502 |
Chain | Residue |
A | PRO102 |
A | ALA103 |
A | SER104 |
A | SER105 |
A | PHE309 |
A | PRO462 |
A | GLU463 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE 3SO A 503 |
Chain | Residue |
A | PHE98 |
A | VAL99 |
A | GLY159 |
A | SER160 |
A | HIS192 |
A | THR249 |
A | ASP274 |
A | ALA276 |
A | ASP303 |
A | HIS305 |
A | LYS306 |
C | HIS120 |
C | LEU336 |
C | LEU339 |
C | TRP349 |
C | THR356 |
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. SIsWdahKWLfQtYGCamVLvK |
Chain | Residue | Details |
D | SER299-LYS320 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:25263219 |
Chain | Residue | Details |
D | LYS306 | |
C | LYS306 | |
B | LYS306 | |
A | LYS306 |