6XDK
Crystal structure of Phosphoserine aminotransferase (SerC) from Stenotrophomonas maltophilia K279a
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006563 | biological_process | L-serine metabolic process |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006563 | biological_process | L-serine metabolic process |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006563 | biological_process | L-serine metabolic process |
| C | 0006564 | biological_process | L-serine biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0008615 | biological_process | pyridoxine biosynthetic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006563 | biological_process | L-serine metabolic process |
| D | 0006564 | biological_process | L-serine biosynthetic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0008615 | biological_process | pyridoxine biosynthetic process |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 400 |
| Chain | Residue |
| A | GLN195 |
| A | PRO200 |
| A | GLY202 |
| B | HOH898 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | HOH505 |
| A | HOH655 |
| A | TRP102 |
| A | THR152 |
| A | ILE153 |
| A | HIS327 |
| A | ARG334 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 401 |
| Chain | Residue |
| A | GLN358 |
| A | ARG359 |
| A | HOH501 |
| A | HOH705 |
| B | GLY111 |
| B | VAL114 |
| B | HOH804 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | TRP102 |
| B | THR152 |
| B | ILE153 |
| B | LYS196 |
| B | HIS327 |
| B | ARG334 |
| B | HOH596 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | PRO131 |
| B | ARG133 |
| B | PHE158 |
| B | HOH522 |
| B | HOH545 |
| B | HOH651 |
| B | HOH740 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 401 |
| Chain | Residue |
| C | GLY111 |
| C | VAL114 |
| C | HOH782 |
| D | ARG359 |
| D | HOH579 |
| D | HOH835 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 402 |
| Chain | Residue |
| C | TRP102 |
| C | THR152 |
| C | ILE153 |
| C | LYS196 |
| C | HIS327 |
| C | ARG334 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 403 |
| Chain | Residue |
| C | LEU130 |
| C | PRO131 |
| C | ARG133 |
| C | PHE158 |
| C | HOH514 |
| C | HOH593 |
| C | HOH613 |
| C | HOH639 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 400 |
| Chain | Residue |
| D | GLN195 |
| D | PRO200 |
| D | GLY202 |
| D | HOH856 |
| site_id | AD1 |
| Number of Residues | 23 |
| Details | binding site for Di-peptide PLP B 404 and LYS B 196 |
| Chain | Residue |
| A | ASN237 |
| A | THR238 |
| B | ALA9 |
| B | ALA12 |
| B | GLY75 |
| B | ALA76 |
| B | THR77 |
| B | TRP102 |
| B | THR152 |
| B | ASP172 |
| B | SER174 |
| B | ALA194 |
| B | GLN195 |
| B | ASN197 |
| B | LEU198 |
| B | GLY199 |
| B | TYR338 |
| B | EDO402 |
| B | HOH519 |
| B | HOH581 |
| B | HOH605 |
| B | HOH608 |
| B | HOH752 |
| site_id | AD2 |
| Number of Residues | 22 |
| Details | binding site for Di-peptide PLP C 404 and LYS C 196 |
| Chain | Residue |
| D | ASN237 |
| D | THR238 |
| C | ALA9 |
| C | ALA12 |
| C | GLY75 |
| C | ALA76 |
| C | THR77 |
| C | TRP102 |
| C | THR152 |
| C | ASP172 |
| C | SER174 |
| C | ALA194 |
| C | GLN195 |
| C | ASN197 |
| C | LEU198 |
| C | GLY199 |
| C | TYR338 |
| C | EDO402 |
| C | HOH532 |
| C | HOH568 |
| C | HOH589 |
| C | HOH592 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 20 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. YGVIyaGAQKnlgpv.GvAvM |
| Chain | Residue | Details |
| A | TYR187-MET206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
