2F5K: Chromo domain of human MRG15

Crystal structure of the chromo domain of human MRG15. Determined by X-ray diffraction at 2.2 Å resolution. Released 14 Nov 2006.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 6
Atoms: 4,571
Mol. weight: 73.51 kDa
Released: 14 Nov 2006

Explore 2F5K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2F5K contains 18 α-helices and 30 β-strands across 6 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: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	16-20	5	1
β-strand	25-36	12	1
β-strand	39-46	8	1
α-helix	51-53	3
β-strand	55-58	4	1
α-helix	59-61	3
β-strand	62-64	3	1
α-helix	67-86	20

Chain B: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	2
β-strand	24-36	13	2
β-strand	39-46	8	2
α-helix	51-53	3
β-strand	55-58	4	2
α-helix	59-61	3
β-strand	62-64	3	2
α-helix	67-84	18

Chain C: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	15-21	7	3
β-strand	24-34	11	3
β-strand	41-44	4	3
α-helix	51-53	3
β-strand	55-58	4	3
α-helix	59-61	3
β-strand	62-64	3	3
α-helix	67-84	18

Chain D: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	4
β-strand	24-35	12	4
β-strand	40-46	7	4
α-helix	51-53	3
β-strand	55-58	4	4
α-helix	59-61	3
β-strand	62-64	3	4
α-helix	67-82	16

Chain E: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	5
β-strand	24-34	11	5
β-strand	41-46	6	5
α-helix	51-53	3
β-strand	55-58	4	5
α-helix	59-61	3
β-strand	62-64	3	5
α-helix	67-81	15

Chain F: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	15-21	7	6
β-strand	24-34	11	6
β-strand	41-44	4	6
α-helix	51-53	3
β-strand	55-58	4	6
α-helix	59-61	3
β-strand	62-64	3	6
α-helix	67-85	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mortality factor 4-like protein 1	A, B, C, D, E, F	protein	102	Homo sapiens	Q9UBU8 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>2F5K_1 Mortality factor 4-like protein 1 (chains A, B, C, D, E, F)
MHHHHHHAMGILMAPKQDPKPKFQEGERVLCFHGPLLYEAKCVKVAIKDKQVKYFIHYSG
WNKNWDEWVPESRVLKYVDTNLQKQRELQKANQEQYAEGKMR

Primary citation

Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3. Zhang, P., Du, J., Sun, B. et al. Nucleic Acids Res (2006) 34:6621-6628. DOI 10.1093/nar/gkl989 · PubMed

Other PDB entries of the same protein (UniProt Q9UBU8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2F5J 2.2 Å, Crystal structure of MRG domain from human MRG15
2AQL 2.3 Å, Crystal Structure of the MRG15 MRG domain
6INE 2.6 Å, Crystal Structure of human ASH1L-MRG15 complex
7S4A 2.69 Å, MRG15 complex with PALB2 peptide
6AGO 3.1 Å, Crystal structure of MRG15-ASH1L Histone methyltransferase complex
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
2EFI Solution structure of the chromo domain of Mortality factor 4-like protein 1 from human
2LKM Structural Basis for Molecular Interactions Involving MRG Domains: Implications in…
2N1D Solution structure of the MRG15-MRGBP complex

Browse structure collections

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