2pfl Summary



The structure was published by Becker, A., Fritz-Wolf, K., Kabsch, W., Knappe, J., Schultz, S., and Volker Wagner, A.F., in 1999 in a paper entitled "Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.9 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 PROTEIN (PYRUVATE FORMATE-LYASE).

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 most likely forms homodimers.

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 PROTEIN (PYRUVATE FORMATE-LYASE) P09373 (2-760) (PFLB_ECOLI)search Escherichia coli K-12search 100% 759 100%
B PROTEIN (PYRUVATE FORMATE-LYASE) P09373 (2-760) (PFLB_ECOLI)search Escherichia coli K-12search 100% 759 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P09373 (2 - 760) PROTEIN (PYRUVATE FORMATE-LYASE) Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P09373) PFL-likesearch Anaerobic Ribonucleotide-triphosphate Reductase Large Chainsearch PF01228: Glycine radicalsearch, PF02901: Pyruvate formate lyasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P09373) protein bindingsearch formate C-acetyltransferase activitysearch transferase activity, transferring acyl groupssearch transferase activitysearch catalytic activitysearch carbohydrate metabolic processsearch anaerobic respirationsearch glucose metabolic processsearch metabolic processsearch membranesearch cytoplasmsearch

Chain InterPro annotation
A, B Glycine radical domainsearch Pyruvate formate lyase domainsearch Formate acetyltransferasesearch Formate C-acetyltransferase glycine radical, conserved sitesearch