2L4Z: Fusion of CtIP (641-685) to LMO4-LIM1

NMR structure of fusion of CtIP (641-685) to LMO4-LIM1 (18-82). Determined by solution NMR. Released 26 Oct 2011.

Method: Solution NMR
Organisms: Homo sapiens, Mus musculus
Chains: 1
Atoms: 913
Mol. weight: 13.35 kDa
Ligands: ZN
Released: 26 Oct 2011

Explore 2L4Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2L4Z contains 3 α-helices and 13 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	651-653	3
β-strand	667	1	1
β-strand	672-673	2	2
β-strand	685	1	3
β-strand	904	1	3
β-strand	22	1	4
β-strand	23	1	2
β-strand	29	1	4
β-strand	35-38	4	2
β-strand	41-44	4	2
β-strand	49	1	5
β-strand	56	1	5
α-helix	57-59	3
β-strand	65	1	1
β-strand	72	1	1
α-helix	74-80	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA endonuclease RBBP8,LIM domain transcription factor LMO4	A	protein	123	Homo sapiens, Mus musculus	P61969 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2L4Z_1 DNA endonuclease RBBP8,LIM domain transcription factor LMO4 (chains A)
GSSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGGGSGGHMGSGGLS
WKRCAGCGGKIADRFLLYAMDSYWHSRCLKCSSCQAQLGDIGTSSYTKSGMILCRNDYIR
LFG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Structural Basis of the Interaction of the Breast Cancer Oncogene LMO4 with the Tumour Suppressor CtIP/RBBP8. Stokes, P.H., Liew, C.W., Kwan, A.H. et al. J Mol Biol (2013) 425:1101-1110. DOI 10.1016/j.jmb.2013.01.017 · PubMed

Other PDB entries of the same protein (UniProt P61969 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2DFY 1.65 Å, Crystal structure of a cyclized protein fusion of LMO4 LIM domains 1 and 2 with the LIM…
2MBV LMO4-LIM2 in complex with DEAF1 (404-418)

Browse structure collections

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