1M19: Histone H3.3C

Ligand binding alters the structure and dynamics of nucleosomal DNA. Determined by X-ray diffraction at 2.3 Å resolution. Released 18 Feb 2003.

Method
X-ray diffraction
Resolution
2.3 Å
Organisms
Synthetic construct, Xenopus laevis
Chains
10
Atoms
13,158
Mol. weight
206.58 kDa
Ligands
ABU, PYB, IMT, MN
Released
18 Feb 2003

Explore 1M19 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M19 contains 41 α-helices and 20 β-strands across 8 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: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix441-4422
α-helix445-45410
α-helix464-47613
β-strand483-48421
α-helix486-51328
β-strand518-51922
α-helix521-53111
Chain B: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix26-283
α-helix31-4010
β-strand45-4622
α-helix50-7526
β-strand80-8121
α-helix83-9210
β-strand96-9833
Chain C: 7 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix817-8215
α-helix827-83610
β-strand842-84324
α-helix846-87227
β-strand877-87825
α-helix880-8889
α-helix891-8966
β-strand900-90236
α-helix913-9153
α-helix9171
Chain D: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix1235-124511
β-strand1250-125125
α-helix1253-128028
β-strand1285-128624
α-helix1288-129811
α-helix1301-131919
Chain E: 5 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix641-6422
α-helix645-65612
α-helix664-67815
β-strand683-68427
α-helix686-71328
β-strand718-71928
α-helix721-73010
Chain F: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix219-2224
α-helix225-2284
α-helix231-24010
β-strand245-24628
α-helix250-27526
β-strand280-28127
α-helix283-29210
β-strand296-29836
Chain G: 7 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix1017-10215
α-helix1027-103610
β-strand1042-104329
α-helix1047-107226
β-strand1077-1078210
α-helix1080-10889
α-helix1091-10966
β-strand1100-110233
α-helix1113-11153
α-helix1117-11182
Chain H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix1435-144511
β-strand1450-1451210
α-helix1453-148028
β-strand1485-148629
α-helix1488-149811
α-helix1501-151919

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Palindromic 146 Base Pair DNA FragmentI, JDNA146Synthetic construct
Histone H3.3CA, Eprotein135Xenopus laevisP02302 (AlphaFold model)
Histone H4B, Fprotein102Xenopus laevisP62799 (AlphaFold model)
Histone H2A type 1C, Gprotein129Xenopus laevisP06897 (AlphaFold model)
Histone H2BD, Hprotein125Xenopus laevisP02281 (AlphaFold model)
Sequence of entity 1 (I, J), FASTA
>1M19_1 Palindromic 146 Base Pair DNA Fragment (chains I, J)
ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGC
ATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT
GGTAGAATCTGCAGGTGGATATTGAT
Sequence of entity 2 (A, E), FASTA
>1M19_2 Histone H3.3C (chains A, E)
ARTKQTARKSTGGKAPRKQLVTKAAKKCAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 3 (B, F), FASTA
>1M19_3 Histone H4 (chains B, F)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 4 (C, G), FASTA
>1M19_4 Histone H2A type 1 (chains C, G)
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT
ESAKSAKSK
Sequence of entity 5 (D, H), FASTA
>1M19_5 Histone H2B (chains D, H)
PEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMS
IMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTK
YTSAK

Ligands and cofactors

IDNameFormulaCopies
ABUGamma-amino-butanoic acidC4 H9 N O25
PYB4-amino-(1-methylpyrrole)-2-carboxylic acidC6 H8 N2 O235
IMT4-amino-(1-methylimidazole)-2-carboxylic acidC5 H7 N3 O25
MNManganese (II) ionMn11
DIB3-amino-(dimethylpropylamine)C5 H14 N25
BALBeta-alanineC3 H7 N O25

Primary citation

Crystal Structures of Nucleosome Core Particles in Complex with Minor Groove DNA-binding Ligands. Suto, R.K., Edayathumangalam, R.S., White, C.L. et al. J Mol Biol (2003) 326:371-380. DOI 10.1016/S0022-2836(02)01407-9 · PubMed

Other PDB entries of the same protein (UniProt P02302 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1M19 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.