4UUZ: MCM2-histone complex

MCM2-histone complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 11 Feb 2015.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: DROSOPHILA MELANOGASTER, HOMO SAPIENS
Chains: 3
Atoms: 1,682
Mol. weight: 34.8 kDa
Released: 11 Feb 2015

Explore 4UUZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4UUZ contains 9 α-helices and 6 β-strands across 3 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, 2 β-strands

Element	Residues	Length	Sheet
α-helix	64-78	15
β-strand	83-84	2	1
α-helix	86-113	28
β-strand	118-119	2	2
α-helix	121-131	11

Chain B: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	25-28	4
α-helix	31-40	10
β-strand	45-46	2	2
α-helix	50-75	26
β-strand	80-81	2	1
α-helix	83-92	10

Chain C: 2 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	70-71	2	2
α-helix	77-80	4
β-strand	95	1	1
α-helix	107-118	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone H3	A	protein	136	DROSOPHILA MELANOGASTER	P02299 (AlphaFold model)
Histone H4	B	protein	103	DROSOPHILA MELANOGASTER	P84040 (AlphaFold model)
DNA replication licensing factor MCM2	C	protein	70	HOMO SAPIENS	P49736 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4UUZ_1 HISTONE H3 (chains A)
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTE
LLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTI
MPKDIQLARRIRGERA

Sequence of entity 2 (B), FASTA

>4UUZ_2 HISTONE H4 (chains B)
MTGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK
VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Sequence of entity 3 (C), FASTA

>4UUZ_3 DNA REPLICATION LICENSING FACTOR MCM2 (chains C)
GEELIGDGMERDYRAIPELDAYEAEGLALDDEDVEELTASQREAAERAMRQRDREAGRGL
GRMRRGLLYD

Primary citation

Structural Insight Into How the Human Helicase Subunit Mcm2 May Act as a Histone Chaperone Together with Asf1 at the Replication Fork. Richet, N., Liu, D., Legrand, P. et al. Nucleic Acids Res (2015) 43:1905. DOI 10.1093/NAR/GKV021 · PubMed

Other PDB entries of the same protein (UniProt P02299 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6AT0 1.28 Å, Chromodomain HP1 with a p-nitro-L-phenylalanine mutation at position 24 bound to histone…
6MHA 1.5 Å, dHP1 Chromodomain Y24W variant bound to histone H3 peptide containing trimethyllysine
6ASZ 1.52 Å, Chromodomain HP1 with Y24F mutation bound to histone H3 peptide containing trimethyl…
7VRF 1.7 Å, Crystal structure of Oxpecker chromodomain in complex with H3K9me3
1KNA 2.1 Å, Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.
9ZQB 2.1 Å, Nucleosome with an SSB at SHL -2.8 in complex with human PARP2 and HPF1, Class 1
2NQB 2.3 Å, Drosophila Nucleosome Structure
9ZQC 2.37 Å, Nucleosome with an SSB at SHL -2.8 in complex with human PARP2 and HPF1, Class 2
1KNE 2.4 Å, Chromo domain of HP1 complexed with histone H3 tail containing trimethyllysine 9
2PYO 2.43 Å, Drosophila nucleosome core
8UX1 2.5 Å, Cryo-EM structure of Ran bound to RCC1 and the nucleosome core particle
4QUF 2.5 Å, crystal structure of chromodomain of Rhino with H3K9me3

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