CRYSTAL STRUCTURE AT 2.4 ANGSTROM RESOLUTION OF E. COLI SERINE HYDROXYMETHYLTRANSFERASE IN COMPLEX WITH GLYCINE AND 5-FORMYL TETRAHYDROFOLATE
The structure was published by Scarsdale, J.N., Radaev, S., Kazanina, G., Schirch, V., and Wright, H.T., in 2000 in a paper entitled "Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of SERINE HYDROXYMETHYLTRANSFERASE.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: