6ZRC: Human RBAP48

Structure of the human RBAP48 in complex with a macrocyclic peptide cyclized via a xylene linker attached to two cysteines. Determined by X-ray diffraction at 2.6 Å resolution. Released 28 Oct 2020.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
4
Atoms
6,335
Mol. weight
99.24 kDa
Ligands
PXY
Released
28 Oct 2020

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

Secondary structure: helices and β-sheets

6ZRC contains 16 α-helices and 54 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: 6 helices, 27 β-strands

ElementResiduesLengthSheet
α-helix11-3121
β-strand32-3981
β-strand48-5472
α-helix55-562
β-strand61-6992
β-strand78-87102
β-strand114-12292
β-strand129-13353
β-strand136-14383
β-strand149-15353
α-helix154-1563
β-strand183-18534
β-strand192-19654
β-strand202-20654
β-strand221-22334
β-strand230-23565
β-strand242-24765
β-strand251-25665
β-strand267-27045
β-strand276-28166
β-strand288-29366
β-strand297-30266
β-strand309-31466
β-strand320-32567
β-strand332-33767
β-strand342-34657
α-helix347-3493
α-helix356-3594
β-strand366-36947
β-strand377-38261
β-strand390-39451
β-strand398-40471
α-helix406-4094
Chain B: 6 helices, 27 β-strands
ElementResiduesLengthSheet
α-helix11-3121
β-strand32-3988
β-strand48-5479
α-helix55-562
β-strand61-6999
β-strand78-87109
β-strand115-12289
β-strand129-133510
β-strand136-143810
β-strand149-153510
α-helix154-1563
β-strand183-185311
β-strand192-196511
β-strand202-206511
β-strand221-223311
β-strand230-235612
β-strand242-247612
β-strand251-256612
β-strand267-270412
β-strand276-281613
β-strand288-293613
β-strand297-302613
β-strand309-314613
β-strand320-325614
β-strand332-337614
β-strand342-346514
α-helix347-3493
α-helix356-3594
β-strand366-369414
β-strand377-38268
β-strand390-39458
β-strand398-40478
α-helix406-4094
Chains P and Q: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-64
α-helix13-142

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone-binding protein RBBP4A, Bprotein427Homo sapiensQ09028 (AlphaFold model)
macrocyclic peptide based on residues 659-672 of the metastasis-associated protein MTA1P, Qprotein16Homo sapiensQ13330 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6ZRC_1 Histone-binding protein RBBP4 (chains A, B)
GPMADKEAAFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTRPEG
KDFSIHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEKGEFGGFGSVSGKIEIE
IKINHEGEVNRARYMPQNPCIIATKTPSSDVLVFDYTKHPSKPDPSGECNPDLRLRGHQK
EGYGLSWNPNLSGHLLSASDDHTICLWDISAVPKEGKVVDAKTIFTGHTAVVEDVSWHLL
HESLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTV
ALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPED
AEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQMAENIYNDEDPEGSV
DPEGQGS
Sequence of entity 2 (P, Q), FASTA
>6ZRC_2 macrocyclic peptide based on residues 659-672 of the metastasis-associated protein MTA1 (chains P, Q)
XCTKRAARRPYKPCAX

Ligands and cofactors

IDNameFormulaCopies
PXYPara-xyleneC8 H102

Primary citation

Structure Based Design of Bicyclic Peptide Inhibitors of RbAp48. Hart, P.'., Hommen, P., Noisier, A. et al. Angew Chem Int Ed Engl (2021) 60:1813-1820. DOI 10.1002/anie.202009749 · PubMed

Other PDB entries of the same protein (UniProt Q09028 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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