3ISL
Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucG) from Bacillus subtilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000256 | biological_process | allantoin catabolic process |
A | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
A | 0005777 | cellular_component | peroxisome |
A | 0006144 | biological_process | purine nucleobase metabolic process |
A | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
A | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0000256 | biological_process | allantoin catabolic process |
B | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
B | 0005777 | cellular_component | peroxisome |
B | 0006144 | biological_process | purine nucleobase metabolic process |
B | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
B | 0019752 | biological_process | carboxylic acid metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PLP A 419 |
Chain | Residue |
A | THR72 |
B | HIS268 |
B | THR269 |
A | SER73 |
A | ARG74 |
A | PHE99 |
A | GLY147 |
A | THR149 |
A | ASP174 |
A | GLN199 |
A | LYS200 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PLP B 419 |
Chain | Residue |
A | THR269 |
B | THR72 |
B | SER73 |
B | ARG74 |
B | PHE99 |
B | GLY147 |
B | THR149 |
B | ASP174 |
B | GLN199 |
B | LYS200 |
Functional Information from PROSITE/UniProt
site_id | PS00595 |
Number of Residues | 21 |
Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDAAigGTQKclsvpsGmApI |
Chain | Residue | Details |
A | ILE191-ILE211 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"20852637","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |