6G16: Histone-binding protein RBBP4

Structure of the human RBBP4:MTA1(464-546) complex showing loop exchange. Determined by X-ray diffraction at 2.8 Å resolution. Released 13 Jun 2018.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Homo sapiens
Chains
8
Atoms
14,642
Mol. weight
229.93 kDa
Released
13 Jun 2018

Explore 6G16 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6G16 contains 46 α-helices and 125 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: 6 helices, 30 β-strands

ElementResiduesLengthSheet
α-helix11-3121
β-strand32-3981
β-strand48-5472
β-strand61-6992
β-strand77-87112
β-strand108-10921
β-strand115-12392
β-strand129-13243
β-strand139-14353
β-strand149-15353
α-helix154-1563
α-helix161-1633
β-strand171-17334
β-strand183-18535
β-strand192-19655
β-strand202-20655
β-strand216-21723
β-strand221-22335
β-strand230-23566
β-strand242-24766
β-strand251-25666
β-strand267-27046
β-strand276-28167
β-strand288-29367
β-strand297-30267
β-strand309-31467
β-strand320-32568
β-strand332-33768
β-strand342-34658
α-helix347-3493
α-helix356-3616
β-strand366-37058
β-strand377-38261
β-strand389-39461
β-strand398-40471
α-helix406-4094
Chains B, D and F: 6 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand472-47431
α-helix477-4859
α-helix487-4904
α-helix492-4954
α-helix502-5032
α-helix505-51410
α-helix534-5429
Chain C: 6 helices, 30 β-strands
ElementResiduesLengthSheet
α-helix11-3121
β-strand32-3989
β-strand47-54810
β-strand61-69910
β-strand77-871110
β-strand108-10929
β-strand115-123910
β-strand129-13244
β-strand139-14354
β-strand149-15354
α-helix154-1563
α-helix161-1633
β-strand171-17333
β-strand183-185311
β-strand192-196511
β-strand202-206511
β-strand216-21724
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-strand311-314413
β-strand320-325614
β-strand332-337614
β-strand342-346514
α-helix347-3493
α-helix356-3616
β-strand366-370514
β-strand377-38269
β-strand389-39469
β-strand398-40479
α-helix406-4094
Chain E: 5 helices, 30 β-strands
ElementResiduesLengthSheet
α-helix12-3120
β-strand32-39815
β-strand47-54816
β-strand61-68816
β-strand77-871116
β-strand108-109215
β-strand115-123916
β-strand129-132417
β-strand139-143517
β-strand149-153517
α-helix154-1563
β-strand171-173318
β-strand183-185319
β-strand192-196519
β-strand202-206519
β-strand216-217217
β-strand221-223319
β-strand230-235620
β-strand242-247620
β-strand251-256620
β-strand267-270420
β-strand276-281621
β-strand288-293621
β-strand298-302521
β-strand311-313321
β-strand320-325622
β-strand332-337622
β-strand342-346522
α-helix347-3493
α-helix356-3616
β-strand366-370522
β-strand377-382615
β-strand389-394615
β-strand398-404715
α-helix406-4094
Chain G: 5 helices, 31 β-strands
ElementResiduesLengthSheet
α-helix11-3121
β-strand32-39823
β-strand47-49324
β-strand54124
β-strand61-69924
β-strand77-871124
β-strand108-109223
β-strand115-123924
β-strand129-132418
β-strand139-143518
β-strand149-153518
α-helix154-1563
β-strand171-173317
β-strand183-185325
β-strand192-196525
β-strand202-206525
β-strand216-217218
β-strand221-223325
β-strand230-235626
β-strand242-247626
β-strand251-256626
β-strand267-270426
β-strand276-281627
β-strand288-293627
β-strand297-302627
β-strand311-314427
β-strand320-325628
β-strand332-337628
β-strand342-346528
α-helix347-3493
α-helix356-3616
β-strand366-370528
β-strand377-382623
β-strand389-394623
β-strand398-404723
α-helix406-4094
Chain H: 6 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand472-474323
α-helix477-4859
α-helix487-4904
α-helix492-4954
α-helix502-5032
α-helix505-51511
α-helix534-5429

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone-binding protein RBBP4A, C, E, Gprotein425Homo sapiensQ09028 (AlphaFold model)
Metastasis-associated protein MTA1B, D, F, Hprotein85Homo sapiensQ13330 (AlphaFold model)
Sequence of entity 1 (A, C, E, G), FASTA
>6G16_1 Histone-binding protein RBBP4 (chains A, C, E, G)
MADKEAAFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTRPEGKD
FSIHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEKGEFGGFGSVSGKIEIEIK
INHEGEVNRARYMPQNPCIIATKTPSSDVLVFDYTKHPSKPDPSGECNPDLRLRGHQKEG
YGLSWNPNLSGHLLSASDDHTICLWDISAVPKEGKVVDAKTIFTGHTAVVEDVSWHLLHE
SLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTVAL
WDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPEDAE
DGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQMAENIYNDEDPEGSVDP
EGQGS
Sequence of entity 2 (B, D, F, H), FASTA
>6G16_2 Metastasis-associated protein MTA1 (chains B, D, F, H)
GAAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQ
SPLVLKQAVRKPLEAVLRYLETHPR

Primary citation

The structure of the core NuRD repression complex provides insights into its interaction with chromatin. Millard, C.J., Varma, N., Saleh, A. et al. Elife (2016) 5:e13941-e13941. DOI 10.7554/eLife.13941 · 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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