9BOW
X-ray structure of Thermus thermophilus serine hydroxymethyltransferase with PLP-L-Ser external aldimine and 5-formyltetrahydrofolate (folinic acid)
Functional Information from PROSITE/UniProt
site_id | PS00096 |
Number of Residues | 17 |
Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVvTSTTHKTLrGPRGG |
Chain | Residue | Details |
A | HIS218-GLY234 | |
B | HIS218-GLY234 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|Ref.2 |
Chain | Residue | Details |
B | TYR51 | |
B | GLY94 | |
B | SER172 | |
B | HIS200 | |
B | HIS225 | |
B | GLY258 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051 |
Chain | Residue | Details |
B | LEU117 | |
B | GLY121 | |
B | GLU242 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051 |
Chain | Residue | Details |
B | HIS225 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.2 |
Chain | Residue | Details |
B | LYS226 |