The structure was published by Phale, P.S., Philippsen, A., Widmer, C., Phale, V.P., Rosenbusch, J.P., and Schirmer, T., in 2001 in a paper entitled "Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation." (abstract).
This crystal structure
was determined using
X-ray diffraction
at a resolution of 2.2 Å and deposited in 2001.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of OUTER MEMBRANE PROTEIN F.
This molecule has the UniProt identifier P02931 (OMPF_ECOLI). The sample contained 340 residues which is 100% of the natural sequence. Out of 340 residues 340 were observed and are deposited in the PDB.
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 homotrimers.
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):
