1q1c Summary

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Crystal structure of N(1-260) of human FKBP52

The structure was published by Wu, B., Li, P., Liu, Y., et al., Bartlam, M., Shen, B., and Rao, Z., in 2004 in a paper entitled "3D structure of human FK506-binding protein 52: Implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2003.

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

The PDB entry contains the structure of FK506-binding protein 4. This molecule has the UniProt identifier Q02790 (FKBP4_HUMAN)search. The sample contained 280 residues which is < 90% of the natural sequence. Out of 280 residues 237 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 is most likely monomeric.

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 FK506-binding protein 4 Q02790 (2-260) (FKBP4_HUMAN)search Homo sapienssearch < 90% 280 84%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q02790 (2 - 260) FK506-binding protein 4 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A FKBP immunophilin/proline isomerasesearch Chitinase A; domain 3search FKBP-type peptidyl-prolyl cis-trans isomerasesearch

Chain ID Biological process (GO)
A (Q02790) protein foldingsearch

Chain InterPro annotation
A Peptidyl-prolyl cis-trans isomerase, FKBP-type, domainsearch Peptidyl-prolyl cis-trans isomerase, FKBP-typesearch