3lpy Summary


Crystal structure of the RRM domain of CyP33

The structure was published by Wang, Z., Song, J., Milne, T.A., et al., Li, H., Allis, C.D., and Patel, D.J., in 2010 in a paper entitled "Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2010.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Peptidyl-prolyl cis-trans isomerase E.

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 Peptidyl-prolyl cis-trans isomerase E Q9UNP9 (5-82) (PPIE_HUMAN)search Homo sapienssearch < 90% 79 100%
B Peptidyl-prolyl cis-trans isomerase E Q9UNP9 (5-82) (PPIE_HUMAN)search Homo sapienssearch < 90% 79 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9UNP9 (5 - 82) Peptidyl-prolyl cis-trans isomerase E Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B Alpha-Beta Plaitssearch RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)search

Chain ID Molecular function (GO)
A, B (Q9UNP9) nucleotide bindingsearch nucleic acid bindingsearch

Chain InterPro annotation
A, B RNA recognition motif domainsearch Nucleotide-binding alpha-beta plait domainsearch