2YBA: Nurf55

Crystal structure of Nurf55 in complex with histone H3. Determined by X-ray diffraction at 2.55 Å resolution. Released 11 May 2011.

Method
X-ray diffraction
Resolution
2.55 Å
Organism
DROSOPHILA MELANOGASTER
Chains
4
Atoms
6,457
Mol. weight
99.68 kDa
Released
11 May 2011

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

Secondary structure: helices and β-sheets

2YBA contains 17 α-helices and 60 β-strands across 4 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: 8 helices, 30 β-strands

ElementResiduesLengthSheet
α-helix12-3524
β-strand36-4381
β-strand52-5982
β-strand65-7392
α-helix801
β-strand81-91112
β-strand119-12792
β-strand133-13753
β-strand140-14783
β-strand153-15753
α-helix158-1603
α-helix165-1662
β-strand175-17843
β-strand187-18934
β-strand196-20054
β-strand206-21054
α-helix214-2152
β-strand21613
β-strand220-22233
β-strand225-22734
β-strand234-23965
β-strand246-25165
β-strand255-26065
β-strand271-27445
β-strand280-28566
β-strand292-29766
β-strand301-30666
β-strand315-31846
β-strand324-32967
β-strand336-34167
β-strand346-35057
α-helix351-3533
α-helix360-3634
β-strand370-37457
β-strand381-38661
β-strand393-39861
β-strand402-40871
α-helix410-4134
Chain B: 7 helices, 30 β-strands
ElementResiduesLengthSheet
α-helix12-3524
β-strand36-4388
β-strand52-5989
β-strand65-7399
β-strand81-91119
β-strand119-12799
β-strand133-137510
β-strand140-147810
β-strand153-157510
α-helix158-1603
α-helix165-1662
β-strand175-178410
β-strand187-189311
β-strand196-200511
β-strand206-210511
α-helix214-2152
β-strand216110
β-strand220-222310
β-strand225-227311
β-strand234-239612
β-strand246-251612
β-strand255-260612
β-strand271-274412
β-strand280-285613
β-strand292-297613
β-strand301-306613
β-strand315-318413
β-strand324-329614
β-strand336-341614
β-strand346-350514
α-helix351-3533
α-helix360-3634
β-strand370-374514
β-strand381-38668
β-strand393-39868
β-strand402-40878
α-helix410-4134
Chains C and D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix3-53

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Probable histone-binding protein CAF1A, Bprotein422DROSOPHILA MELANOGASTERQ24572 (AlphaFold model)
Histone H3C, Dprotein19DROSOPHILA MELANOGASTERP02299 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2YBA_1 PROBABLE HISTONE-BINDING PROTEIN CAF1 (chains A, B)
GGGRMVDRSDNAAESFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPD
VTKQDGKDYSVHRLILGTHTSDEQNHLLIASVQLPSEDAQFDGSHYDNEKGEFGGFGSVC
GKIEIEIKINHEGEVNRARYMPQNACVIATKTPSSDVLVFDYTKHPSKPEPSGECQPDLR
LRGHQKEGYGLSWNPNLNGYLLSASDDHTICLWDINATPKEHRVIDAKNIFTGHTAVVED
VAWHLLHESLFGSVADDQKLMIWDTRNNNTSKPSHTVDAHTAEVNCLSFNPYSEFILATG
SADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLHVWDLSKIGE
EQSTEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWIICSVSEDNIMQVWQMAENVYNDE
EP
Sequence of entity 2 (C, D), FASTA
>2YBA_2 HISTONE H3 (chains C, D)
ARTKQTARKSTGGKAPRKQ

Primary citation

Histone Methylation by Prc2 is Inhibited by Active Chromatin Marks. Schmitges, F.W., Prusty, A.B., Faty, M. et al. Mol Cell (2011) 42:330. DOI 10.1016/J.MOLCEL.2011.03.025 · PubMed

Other PDB entries of the same protein (UniProt Q24572 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 2YBA 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.