9GMR: SIRT7-H3K36MTUnucleosome complex
SIRT7-H3K36MTUnucleosome complex. Determined by electron microscopy at 2.8 Å resolution. Released 29 Jan 2025.
- Method
- Electron microscopy
- Resolution
- 2.8 Å
- Organism
- Homo sapiens
- Chains
- 11
- Atoms
- 14,763
- Mol. weight
- 247.19 kDa
- Ligands
- ZN, A1IY0
- Released
- 29 Jan 2025
Explore 9GMR in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9GMR contains 51 α-helices and 33 β-strands across 9 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: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-55 | 11 | |
| α-helix | 64-75 | 12 | |
| β-strand | 83-84 | 2 | 1 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 2 |
| α-helix | 121-131 | 11 | |
Chain B: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 2 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 1 |
| α-helix | 83-91 | 9 | |
| β-strand | 96-98 | 3 | 3 |
Chain C: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-35 | 8 | |
| β-strand | 42-43 | 2 | 4 |
| α-helix | 47-71 | 25 | |
| β-strand | 77-78 | 2 | 5 |
| α-helix | 80-89 | 10 | |
| α-helix | 91-96 | 6 | |
| β-strand | 101-102 | 2 | 6 |
Chains D and H: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-48 | 11 | |
| β-strand | 53-54 | 2 | 5 |
| α-helix | 56-83 | 28 | |
| β-strand | 88-89 | 2 | 4 |
| α-helix | 91-101 | 11 | |
| α-helix | 105-123 | 19 | |
Chain E: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-55 | 11 | |
| α-helix | 64-75 | 12 | |
| β-strand | 83-84 | 2 | 7 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 8 |
| α-helix | 121-130 | 10 | |
Chain F: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 8 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 7 |
| α-helix | 83-92 | 10 | |
| β-strand | 97-98 | 2 | 6 |
Chain G: 6 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-20 | 4 | |
| α-helix | 28-35 | 8 | |
| β-strand | 42-43 | 2 | 9 |
| α-helix | 47-72 | 26 | |
| β-strand | 77-78 | 2 | 10 |
| α-helix | 80-88 | 9 | |
| α-helix | 91-96 | 6 | |
| β-strand | 100-102 | 3 | 3 |
| α-helix | 113-115 | 3 | |
Chain K: 17 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-36 | 20 | |
| α-helix | 51-53 | 3 | |
| α-helix | 55-73 | 19 | |
| α-helix | 82-98 | 17 | |
| β-strand | 102-106 | 5 | 11 |
| α-helix | 110-114 | 5 | |
| α-helix | 147-156 | 10 | |
| β-strand | 163-166 | 4 | 11 |
| α-helix | 172-176 | 5 | |
| α-helix | 180-182 | 3 | |
| β-strand | 183-185 | 3 | 11 |
| β-strand | 192-195 | 4 | 12 |
| β-strand | 202-205 | 4 | 12 |
| β-strand | 215 | 1 | 13 |
| β-strand | 218 | 1 | 13 |
| β-strand | 233 | 1 | 12 |
| α-helix | 253-260 | 8 | |
| β-strand | 263-267 | 5 | 11 |
| α-helix | 274-276 | 3 | |
| α-helix | 278-281 | 4 | |
| α-helix | 291 | 1 | |
| β-strand | 292-293 | 2 | 11 |
| β-strand | 296 | 1 | 11 |
| α-helix | 304-306 | 3 | |
| β-strand | 311 | 1 | 11 |
| α-helix | 315-326 | 12 | |
| α-helix | 340-343 | 4 | |
| β-strand | 344 | 1 | 12 |
| α-helix | 345-348 | 4 | |
| α-helix | 352-354 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone H3.2 | A, E | protein | 136 | Homo sapiens | Q71DI3 (AlphaFold model) |
| Histone H4 | B, F | protein | 103 | Homo sapiens | P62805 (AlphaFold model) |
| Histone H2A type 2-A | C, G | protein | 129 | Homo sapiens | Q6FI13 (AlphaFold model) |
| Histone H2B type 1-J | D, H | protein | 126 | Homo sapiens | P06899 (AlphaFold model) |
| DNA (149-mer) | I | DNA | 149 | Homo sapiens | |
| DNA (149-mer) | J | DNA | 149 | Homo sapiens | |
| NAD-dependent protein deacetylase sirtuin-7 | K | protein | 401 | Homo sapiens | Q9NRC8 |
Sequence of entity 1 (A, E), FASTA
>9GMR_1 Histone H3.2 (chains A, E)
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVCLREIRRYQKSTE
LLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLAAIHAKRVTI
MPKDIQLARRIRGERA
Sequence of entity 2 (B, F), FASTA
>9GMR_2 Histone H4 (chains B, F)
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK
VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C, G), FASTA
>9GMR_3 Histone H2A type 2-A (chains C, G)
SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKT
ESHHKAKGK
Sequence of entity 4 (D, H), FASTA
>9GMR_4 Histone H2B type 1-J (chains D, H)
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKKSRKESYSIYVYKVLKQVHPDTGISSKAM
GIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT
KYTSAK
Sequence of entity 5 (I), FASTA
>9GMR_5 DNA (149-MER) (chains I)
AGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGC
ACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCA
CGTGTCAGATATATACAAGATCCCCTTAC
Sequence of entity 6 (J), FASTA
>9GMR_6 DNA (149-MER) (chains J)
GTAAGGGGATCTTGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCTTGGC
GGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTACGAC
CAATTGAGCGGCCTCGGCACCGGGATTCT
Sequence of entity 7 (K), FASTA
>9GMR_7 NAD-dependent protein deacetylase sirtuin-7 (chains K)
GMAAGGLSRSERKAAERVRRLREEQQRERLRQVSRILRKAAAERSAEEGRLLAESADLVT
ELQGRSRRREGLKRRQEEVCDDPEELRGKVRELASAVRNAKYLVVYTGAGISTAASIPDY
RGPNGVWTLLQKGRSVSAADLSEAEPTLTHMSITRLHEQKLVQHVVSQNCDGLHLRSGLP
RTAISELHGNMYIEVCTSCVPNREYVRVFDVTERTALHRHQTGRTCHKCGTQLRDTIVHF
GERGTLGQPLNWEAATEAASRADTILCLGSSLKVLKKYPRLWCMTKPPSRRPKLYIVNLQ
WTPKDDWAALKLHGKCDDVMRLLMAELGLEIPAYSRWQDPIFSLATPLRAGEEGSHSRKS
LCRSREEAPPGDRGAPLSSAPILGGWFGRGCTKRTKRKKVT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 1 |
| A1IY0 | [[(2~{R},3~{a}~{R},5~{R},6~{R},6~{a}~{R})-2-(methylamino)-6-oxidanyl-2-(propyla… | C20 H33 N7 O13 P2 S | 1 |
Primary citation
Structural basis of SIRT7 nucleosome engagement and substrate specificity. Moreno-Yruela, C., Ekundayo, B.E., Foteva, P.N. et al. Nat Commun (2025) 16:1328-1328. DOI 10.1038/s41467-025-56529-y · PubMed
Other PDB entries of the same protein (UniProt Q71DI3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2X4W 1.5 Å, Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.
- 4MZG 1.7 Å, Crystal structure of human Spindlin1 bound to histone H3K4me3 peptide
- 2X4Y 1.7 Å, Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.
- 2X4X 1.85 Å, Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.
- 4OUC 1.9 Å, Structure of human haspin in complex with histone H3 substrate
- 5VAC 1.95 Å, Crystal Structure of ATXR5 SET domain in complex with K36me3 histone H3 peptide
- 6ACE 1.98 Å, histone lysine desuccinylase Sirt5 in complex with succinyl peptide H3K122
- 7UVA 1.98 Å, Crystal structure of KDM2A histone demethylase catalytic domain in complex with an H3C36…
- 5B0Z 1.99 Å, The crystal structure of the nucleosome containing H3.2, at 1.98 A resolution
- 3R93 2.06 Å, Crystal structure of the chromo domain of M-phase phosphoprotein 8 bound to H3K9Me3…
- 4MZF 2.1 Å, Crystal structure of human Spindlin1 bound to histone H3(K4me3-R8me2a) peptide
- 4MZH 2.2 Å, Crystal structure of human Spindlin1 bound to histone H3(K4me3-R8me2s) peptide
Browse structure collections
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