6RXM: CobB Ac2

Crystal structure of CobB Ac2 (A76G, I131C, V162G) in complex with H4K16-Acetyl peptide. Determined by X-ray diffraction at 1.92 Å resolution. Released 15 Apr 2020.

Method
X-ray diffraction
Resolution
1.92 Å
Organisms
Escherichia coli (strain K12), Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains
12
Atoms
12,179
Mol. weight
176.58 kDa
Ligands
ZN
Released
15 Apr 2020

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

Secondary structure: helices and β-sheets

6RXM contains 86 α-helices and 89 β-strands across 12 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: 14 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand43-4751
α-helix50-534
α-helix57-593
β-strand6312
β-strand66-6722
β-strand70-7122
α-helix72-754
α-helix78-836
α-helix85-9915
α-helix108-12013
α-helix121-1233
β-strand124-12851
α-helix134-1385
β-strand144-14521
β-strand148-15583
β-strand161-16333
β-strand17314
β-strand18214
β-strand183-18753
α-helix188-1892
α-helix193-1942
α-helix197-20610
β-strand209-21351
β-strand219-22025
α-helix222-2243
α-helix225-2317
β-strand235-24061
β-strand252-25541
α-helix258-27114
Chain B: 14 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand43-4756
α-helix49-513
α-helix53-553
β-strand6117
β-strand66-6727
β-strand70-7127
α-helix72-754
α-helix78-836
α-helix85-9915
α-helix108-12013
α-helix121-1233
β-strand124-12856
α-helix134-1385
β-strand144-14526
β-strand148-15588
β-strand161-16338
β-strand17319
β-strand18219
β-strand183-18758
α-helix188-1892
α-helix193-1942
α-helix197-20610
β-strand209-21356
β-strand219-220210
α-helix222-2243
α-helix225-2317
β-strand235-24066
β-strand252-25546
α-helix258-27013
Chain C: 14 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand43-47511
α-helix49-513
α-helix53-553
β-strand61112
β-strand66-67212
β-strand70-71212
α-helix72-754
α-helix78-836
α-helix85-9915
α-helix108-12013
α-helix121-1233
β-strand124-128511
α-helix134-1385
β-strand144-145211
β-strand148-155813
β-strand161-163313
β-strand173114
β-strand182114
β-strand183-187513
α-helix188-1892
α-helix193-1942
α-helix197-20610
β-strand209-213511
β-strand219-220215
α-helix222-2243
α-helix225-2317
β-strand235-240611
β-strand252-255411
α-helix258-27114
Chain D: 13 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand43-47516
α-helix49-557
α-helix72-754
α-helix78-836
α-helix85-9915
α-helix108-12013
α-helix121-1233
β-strand124-128516
α-helix134-1385
β-strand144-145216
β-strand148-155817
β-strand161-163317
β-strand173118
β-strand182118
β-strand183-187517
α-helix188-1892
α-helix193-1942
α-helix197-20610
β-strand209-213516
β-strand219-220219
α-helix222-2243
α-helix225-2317
β-strand235-240616
β-strand252-255416
α-helix258-27114
Chain E: 15 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand43-47520
α-helix49-557
α-helix57-604
β-strand66-67221
β-strand70-71221
α-helix72-754
α-helix78-836
α-helix85-9915
α-helix108-12013
α-helix121-1233
β-strand124-128520
α-helix134-1385
β-strand144-145220
β-strand148-155822
β-strand161-163322
β-strand173123
β-strand182123
β-strand183-187522
α-helix188-1892
α-helix193-1942
α-helix197-20610
β-strand209-213520
β-strand219-220224
α-helix222-2243
α-helix225-2317
β-strand235-240620
α-helix247-2493
β-strand252-255420
α-helix258-27114
Chain F: 15 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand43-47525
α-helix49-513
α-helix53-553
α-helix72-754
α-helix78-836
α-helix85-9915
α-helix108-12013
α-helix121-1233
β-strand124-128525
α-helix134-1385
β-strand144-145225
β-strand148-155826
β-strand161-163326
β-strand173127
β-strand182127
β-strand183-187526
α-helix188-1892
α-helix193-1942
α-helix197-20610
β-strand209-213525
β-strand219-220228
α-helix222-2243
α-helix225-2317
β-strand235-240625
α-helix247-2493
β-strand252-255425
α-helix258-27013
Chains G, H, I, J and L: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand17-1825
Chain K: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand17-18224
α-helix19-202

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
NAD-dependent protein deacylaseA, B, C, D, E, Fprotein254Escherichia coli (strain K12)P75960 (AlphaFold model)
Histone H4G, H, I, J, K, Lprotein11Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P02309 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>6RXM_1 NAD-dependent protein deacylase (chains A, B, C, D, E, F)
MGSSHHHHHHSQDPKPRVLVLTGAGISAESGIRTFRAADGLWEEHRVEDVGTPEGFDRDP
ELVQAFYNARRRQLQQPEIQPNAAHLALAKLQDALGDRFLLVTQNCDNLHERAGNTNVIH
MHGELLKVRCSQSGQALDWTGDVTPEDKCHCCQFPAPLRPHVVWFGEMPLGMDEIYMALS
MADIFIAIGTSGHVYPAAGFVHEAKLHGAHTVELNLEPSQVGNEFAEKYYGPASQVVPEF
VEKLLKGLKAGSIA
Sequence of entity 2 (G, H, I, J, K, L), FASTA
>6RXM_2 Histone H4 (chains G, H, I, J, K, L)
KGGAKRHRKIL

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn6

Primary citation

Evolved, Selective Erasers of Distinct Lysine Acylations. Spinck, M., Neumann-Staubitz, P., Ecke, M. et al. Angew Chem Int Ed Engl (2020) 59:11142-11149. DOI 10.1002/anie.202002899 · PubMed

Other PDB entries of the same protein (UniProt P75960 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 6RXM 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.