4H65
Crystal structure of SeMet derivative of HMP synthase Thi5 from S. cerevisiae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003674 | molecular_function | molecular_function |
A | 0005506 | molecular_function | iron ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005575 | cellular_component | cellular_component |
A | 0009228 | biological_process | thiamine biosynthetic process |
A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0106344 | molecular_function | 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP |
B | 0003674 | molecular_function | molecular_function |
B | 0005506 | molecular_function | iron ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005575 | cellular_component | cellular_component |
B | 0009228 | biological_process | thiamine biosynthetic process |
B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0106344 | molecular_function | 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:23048037 |
Chain | Residue | Details |
A | HIS66 | |
B | HIS66 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23048037 |
Chain | Residue | Details |
A | GLY115 | |
B | GLY115 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:23048037 |
Chain | Residue | Details |
A | LYS62 | |
B | LYS62 |