3u85 Summary


Crystal structure of human menin in complex with MLL1

The structure was published by Huang, J., Gurung, B., Wan, B., et al., Merchant, J.L., Hua, X., and Lei, M., in 2012 in a paper entitled "The same pocket in menin binds both MLL and JUND but has opposite effects on transcription." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2011.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Menin and Histone-lysine N-methyltransferase MLL.

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 Menin O00255 (2-615) (MEN1_HUMAN)search Homo sapienssearch < 90% 550 88%
B Histone-lysine N-methyltransferase MLL Q03164 (6-25) (KMT2A_HUMAN)search Homo sapienssearch < 90% 21 42%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
O00255 (2 - 615) Menin Homo sapiens
Q03164 (6 - 25) Histone-lysine N-methyltransferase MLL Homo sapiens

Chain Sequence family (Pfam)
A Meninsearch

Chain ID Cellular component (GO)
A (O00255) nucleussearch

Chain InterPro annotation
A Meninsearch