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 | 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 | 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 | 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 | 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: BINDING => ECO:0000255|HAMAP-Rule:MF_00160 |
Chain | Residue | Details |
A | ARG42 | |
B | TRP102 | |
B | THR152 | |
B | ASP172 | |
B | GLN195 | |
B | ASN237 | |
C | ARG42 | |
C | ALA76 | |
C | TRP102 | |
C | THR152 | |
C | ASP172 | |
A | ALA76 | |
C | GLN195 | |
C | ASN237 | |
D | ARG42 | |
D | ALA76 | |
D | TRP102 | |
D | THR152 | |
D | ASP172 | |
D | GLN195 | |
D | ASN237 | |
A | TRP102 | |
A | THR152 | |
A | ASP172 | |
A | GLN195 | |
A | ASN237 | |
B | ARG42 | |
B | ALA76 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00160 |
Chain | Residue | Details |
A | LYS196 | |
B | LYS196 | |
C | LYS196 | |
D | LYS196 |