2YB8: Nurf55

Crystal structure of Nurf55 in complex with Su(z)12. Determined by X-ray diffraction at 2.3 Å resolution. Released 18 May 2011.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
DROSOPHILA MELANOGASTER
Chains
2
Atoms
3,231
Mol. weight
49.65 kDa
Released
18 May 2011

Explore 2YB8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2YB8 contains 8 α-helices and 30 β-strands across 2 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: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix84-863
α-helix88-903
Chain B: 6 helices, 30 β-strands
ElementResiduesLengthSheet
α-helix17-3519
β-strand36-4381
β-strand51-5992
β-strand65-7392
β-strand81-91112
β-strand119-12792
β-strand133-13753
β-strand140-14783
β-strand153-15753
α-helix158-1603
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-strand256-26055
β-strand271-27335
β-strand280-28566
β-strand292-29766
β-strand301-30666
β-strand315-31846
β-strand326-32947
β-strand336-34057
β-strand346-35057
α-helix351-3533
α-helix362-3643
β-strand370-37457
β-strand381-38661
β-strand393-39861
β-strand402-40871
α-helix410-4134

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Polycomb protein SU(Z)12Aprotein13DROSOPHILA MELANOGASTERQ9NJG9 (AlphaFold model)
Probable histone-binding protein CAF1Bprotein422DROSOPHILA MELANOGASTERQ24572 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2YB8_1 POLYCOMB PROTEIN SU(Z)12 (chains A)
NPIFLNRTLSYMK
Sequence of entity 2 (B), FASTA
>2YB8_2 PROBABLE HISTONE-BINDING PROTEIN CAF1 (chains B)
GGGRMVDRSDNAAESFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPD
VTKQDGKDYSVHRLILGTHTSDEQNHLLIASVQLPSEDAQFDGSHYDNEKGEFGGFGSVC
GKIEIEIKINHEGEVNRARYMPQNACVIATKTPSSDVLVFDYTKHPSKPEPSGECQPDLR
LRGHQKEGYGLSWNPNLNGYLLSASDDHTICLWDINATPKEHRVIDAKNIFTGHTAVVED
VAWHLLHESLFGSVADDQKLMIWDTRNNNTSKPSHTVDAHTAEVNCLSFNPYSEFILATG
SADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLHVWDLSKIGE
EQSTEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWIICSVSEDNIMQVWQMAENVYNDE
EP

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

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