4CBS
X-ray structure of quintuple mutant of human alanine glyoxylate aminotransferase, AGXT_RHEAM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005782 | cellular_component | peroxisomal matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006563 | biological_process | L-serine metabolic process |
| A | 0007219 | biological_process | Notch signaling pathway |
| A | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009436 | biological_process | glyoxylate catabolic process |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| A | 0019448 | biological_process | L-cysteine catabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042853 | biological_process | L-alanine catabolic process |
| A | 0046487 | biological_process | glyoxylate metabolic process |
| A | 0046724 | biological_process | oxalic acid secretion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 1389 |
| Chain | Residue |
| A | SER81 |
| A | GLN208 |
| A | LYS209 |
| A | TYR260 |
| A | HIS262 |
| A | THR263 |
| A | GLY82 |
| A | HIS83 |
| A | TRP108 |
| A | GLY156 |
| A | SER158 |
| A | ASP183 |
| A | VAL185 |
| A | ALA186 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 21 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDILysGSQKalnappGtSlI |
| Chain | Residue | Details |
| A | ILE200-ILE220 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"O35423","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O35423","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
