1dfo Summary

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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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A SERINE HYDROXYMETHYLTRANSFERASE P0A825 (1-417) (GLYA_ECOLI)search Escherichia coli K-12search 100% 417 100%
B SERINE HYDROXYMETHYLTRANSFERASE P0A825 (1-417) (GLYA_ECOLI)search Escherichia coli K-12search 100% 417 100%
C SERINE HYDROXYMETHYLTRANSFERASE P0A825 (1-417) (GLYA_ECOLI)search Escherichia coli K-12search 100% 417 100%
D SERINE HYDROXYMETHYLTRANSFERASE P0A825 (1-417) (GLYA_ECOLI)search Escherichia coli K-12search 100% 417 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0A825 (1 - 417) SERINE HYDROXYMETHYLTRANSFERASE Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P0A825) GABA-aminotransferase-likesearch Type I PLP-dependent aspartate aminotransferase-like (Major domain)search, Aspartate Aminotransferase, domain 1search PF00464: Serine hydroxymethyltransferasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B, C, D (P0A825) pyridoxal phosphate bindingsearch catalytic activitysearch glycine hydroxymethyltransferase activitysearch identical protein bindingsearch zinc ion bindingsearch transferase activitysearch glycine metabolic processsearch L-serine metabolic processsearch glycine biosynthetic processsearch glycine biosynthetic process from serinesearch L-serine catabolic processsearch one-carbon metabolic processsearch cellular amino acid biosynthetic processsearch glycine catabolic processsearch tetrahydrofolate interconversionsearch cytoplasmsearch membranesearch cytosolsearch

Chain InterPro annotation
A, B, C, D Serine hydroxymethyltransferasesearch Pyridoxal phosphate-dependent transferase, major region, subdomain 1search Pyridoxal phosphate-dependent transferase, major region, subdomain 2search Pyridoxal phosphate-dependent transferasesearch Serine hydroxymethyltransferase, pyridoxal phosphate binding sitesearch