6M2M: Probable histone H2A.3

Name: PDB 6M2M: A role for histone chaperone OsChz1 in histone recognition and deposition
Published: 2020-10-21
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

A role for histone chaperone OsChz1 in histone recognition and deposition. Determined by X-ray diffraction at 2.85 Å resolution. Released 21 Oct 2020.

Method: X-ray diffraction
Resolution: 2.85 Å
Organisms: Arabidopsis thaliana, Oryza sativa subsp. japonica
Chains: 15
Atoms: 8,020
Mol. weight: 161.12 kDa
Released: 21 Oct 2020

Explore 6M2M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6M2M contains 57 α-helices and 20 β-strands across 15 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.

Chains A and C: 6 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	19-22	4
α-helix	29-38	10
β-strand	44-45	2	3
α-helix	48-74	27
β-strand	79-80	2	4
α-helix	82-90	9
α-helix	93-99	7
α-helix	102-103	2

Chain B: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	62-72	11
β-strand	77-78	2	4
α-helix	80-107	28
β-strand	112-113	2	10
α-helix	115-125	11
α-helix	129-142	14

Chain D: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	62-72	11
α-helix	80-108	29
β-strand	112-113	2	5
α-helix	115-125	11
α-helix	128-146	19

Chain E: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-23	6
α-helix	29-38	10
β-strand	44-45	2	1
α-helix	48-74	27
β-strand	79-80	2	2
α-helix	82-91	10
α-helix	93-99	7

Chain F: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	62-72	11
β-strand	77-78	2	2
α-helix	80-106	27
β-strand	112-113	2	8
α-helix	115-125	11
α-helix	129-143	15

Chain G: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	29-37	9
β-strand	44-45	2	7
α-helix	48-73	26
α-helix	82-91	10
α-helix	93-98	6

Chain H: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	62-72	11
β-strand	77-78	2	6
α-helix	80-106	27
β-strand	112-113	2	7
α-helix	115-125	11
α-helix	129-142	14

Chain I: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	29-38	10
β-strand	44-45	2	8
α-helix	48-73	26
β-strand	80	1	9
α-helix	82-91	10
α-helix	93-99	7

5 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Probable histone H2A.3	A, C, E, G, I, K	protein	93	Arabidopsis thaliana	O81826 (AlphaFold model)
Histone H2B.1	B, D, F, H, J, L	protein	98	Arabidopsis thaliana	Q9LQQ4 (AlphaFold model)
Expressed protein	M, N, O	protein	105	Oryza sativa subsp. japonica	Q2R2Z3 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, I, K), FASTA

>6M2M_1 Probable histone H2A.3 (chains A, C, E, G, I, K)
KKSTSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLAAVLEYLAAEVLELAGNAAR
DNKKTRIVPRHIQLAVRNDEELSKLLGDVTIAN

Sequence of entity 2 (B, D, F, H, J, L), FASTA

>6M2M_2 Histone H2B.1 (chains B, D, F, H, J, L)
KKRSKKNVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAQESSKLARYNKK
PTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS

Sequence of entity 3 (M, N, O), FASTA

>6M2M_3 Expressed protein (chains M, N, O)
ILEKEGLSTNPSEKEIKAVKKRKERAKELEGIDMSNIITSSRRRSTSNFIPLPTPKIVAD
SDEDDEEDAEDDNDEEVNVEGGDEGDNDVGKAGDGSADDAEHDSD

Primary citation

OsChz1 acts as a histone chaperone in modulating chromatin organization and genome function in rice. Du, K., Luo, Q., Yin, L. et al. Nat Commun (2020) 11:5717-5717. DOI 10.1038/s41467-020-19586-z · PubMed

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