2LKM: PHD finger protein 12

Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology. Determined by solution NMR. Released 18 Jan 2012.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 1,736
Mol. weight: 24.59 kDa
Released: 18 Jan 2012

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

Secondary structure: helices and β-sheets

2LKM contains 10 α-helices and 4 β-strands across 2 chains. 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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	207-217	11

Chain B: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	165-172	8
α-helix	173-177	5
β-strand	180-181	2	1
β-strand	189	1	2
α-helix	190-204	15
α-helix	211-228	18
α-helix	236-238	3
α-helix	239-248	10
β-strand	259	1	2
α-helix	260-276	17
α-helix	281-299	19
β-strand	312-313	2	1
α-helix	316-319	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PHD finger protein 12	A	protein	42	Homo sapiens	Q96QT6 (AlphaFold model)
Mortality factor 4-like protein 1	B	protein	172	Homo sapiens	Q9UBU8 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2LKM_1 PHD finger protein 12 (chains A)
DYVQPQLRRPFELLIAAAMERNPTQFQLPNELTCTTALPGSS

Sequence of entity 2 (B), FASTA

>2LKM_2 Mortality factor 4-like protein 1 (chains B)
SNAEVKVKIPEELKPWLVDDWDLITRQKQLFYLPAKKNVDSILEDYANYRKSRGNTDNKE
YAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILADHPDAPMSQVYGAPHLLRLFVRIG
AMLAYTPLDEKSLALLLNYLHDFLKYLAKNSATLFSASDYEVAPPEYHRKAV

Primary citation

Structural basis for molecular interactions involving MRG domains: implications in chromatin biology. Xie, T., Graveline, R., Kumar, G.S. et al. Structure (2012) 20:151-160. DOI 10.1016/j.str.2011.10.019 · PubMed

Other PDB entries of the same protein (UniProt Q96QT6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8BPB 2.8 Å, Cryo-EM structure of the human SIN3B histone deacetylase core complex at 2.8 Angstrom
8BPC 2.8 Å, Cryo-EM structure of the human SIN3B histone deacetylase core complex with SAHA at 2.8…
8C60 3.4 Å, Cryo-EM structure of the human SIN3B full-length complex at 3.4 Angstrom resolution
8BPA 3.7 Å, Cryo-EM structure of the human SIN3B histone deacetylase complex at 3.7 Angstrom
2L9S Solution structure of Pf1 SID1-mSin3A PAH2 Complex

Browse structure collections

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