9EOZ: Human OGG1
Human OGG1 bound to a nucleosome core particle with 8-oxodGuo lesion at SHL6.0. Determined by electron microscopy at 3.1 Å resolution. Released 6 Nov 2024.
- Method
- Electron microscopy
- Resolution
- 3.1 Å
- Organisms
- Homo sapiens, synthetic construct
- Chains
- 11
- Atoms
- 14,100
- Mol. weight
- 238.23 kDa
- Released
- 6 Nov 2024
Explore 9EOZ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9EOZ contains 54 α-helices and 27 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: 16 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26 | 1 | 1 |
| α-helix | 30-32 | 3 | |
| α-helix | 35-38 | 4 | |
| β-strand | 48-51 | 4 | 1 |
| β-strand | 54-59 | 6 | 1 |
| β-strand | 62-68 | 7 | 1 |
| β-strand | 73-77 | 5 | 1 |
| α-helix | 90-100 | 11 | |
| α-helix | 107-109 | 3 | |
| α-helix | 110-116 | 7 | |
| α-helix | 118-126 | 9 | |
| α-helix | 137-145 | 9 | |
| α-helix | 152-165 | 14 | |
| β-strand | 169 | 1 | 2 |
| β-strand | 179 | 1 | 2 |
| α-helix | 194-197 | 4 | |
| α-helix | 204-217 | 14 | |
| α-helix | 221-229 | 9 | |
| α-helix | 233-241 | 9 | |
| α-helix | 248-256 | 9 | |
| α-helix | 269-278 | 10 | |
| α-helix | 293-307 | 15 | |
| α-helix | 311-319 | 9 | |
Chain B: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-28 | 4 | |
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 3 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 4 |
| α-helix | 83-92 | 10 | |
| β-strand | 97-98 | 2 | 5 |
Chain E: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 41-42 | 2 | |
| α-helix | 45-56 | 12 | |
| α-helix | 64-78 | 15 | |
| β-strand | 83-84 | 2 | 6 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 7 |
| 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 | 7 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 6 |
| α-helix | 83-92 | 10 | |
| β-strand | 97-98 | 2 | 8 |
Chain G: 6 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-21 | 5 | |
| α-helix | 27-36 | 10 | |
| β-strand | 42-43 | 2 | 9 |
| α-helix | 47-72 | 26 | |
| β-strand | 77-78 | 2 | 10 |
| α-helix | 80-89 | 10 | |
| α-helix | 93-96 | 4 | |
| β-strand | 101-102 | 2 | 5 |
| α-helix | 113-115 | 3 | |
Chain H: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 35-45 | 11 | |
| β-strand | 50-51 | 2 | 10 |
| α-helix | 53-80 | 28 | |
| β-strand | 85-86 | 2 | 9 |
| α-helix | 88-98 | 11 | |
| α-helix | 102-119 | 18 | |
Chain K: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 41-42 | 2 | |
| α-helix | 45-56 | 12 | |
| α-helix | 64-76 | 13 | |
| β-strand | 83-84 | 2 | 4 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 3 |
| α-helix | 121-131 | 11 | |
Chain L: 6 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-21 | 5 | |
| α-helix | 27-36 | 10 | |
| β-strand | 42-43 | 2 | 11 |
| α-helix | 46-72 | 27 | |
| β-strand | 77-78 | 2 | 12 |
| α-helix | 80-89 | 10 | |
| α-helix | 91-96 | 6 | |
| β-strand | 101-102 | 2 | 8 |
| α-helix | 113-115 | 3 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| N-glycosylase/DNA lyase | A | protein | 356 | Homo sapiens | O15527 (AlphaFold model) |
| Histone H4 | B, F | protein | 102 | Homo sapiens | P62805 (AlphaFold model) |
| Histone H3.3 | E, K | protein | 135 | Homo sapiens | P84243 (AlphaFold model) |
| Histone H2A type 1-C | G, L | protein | 129 | Homo sapiens | Q93077 (AlphaFold model) |
| Histone H2B type 1-C/E/F/G/I | H, M | protein | 125 | Homo sapiens | P62807 |
| Widom 601 DNA (145-MER) | Y | DNA | 145 | synthetic construct | |
| Widom 601 DNA (145-MER) | Z | DNA | 145 | synthetic construct | |
Sequence of entity 1 (A), FASTA
>9EOZ_1 N-glycosylase/DNA lyase (chains A)
GSSHHHHHHSQDPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWRE
QSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQL
YHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPR
LIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLR
ESSYEEAHKALCILPGVGTQVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAK
GPSPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQSRHAQEPPAKRRKGSKGPEG
Sequence of entity 2 (B, F), FASTA
>9EOZ_2 Histone H4 (chains B, F)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (E, K), FASTA
>9EOZ_3 Histone H3.3 (chains E, K)
ARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 4 (G, L), FASTA
>9EOZ_4 Histone H2A type 1-C (chains G, L)
SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKT
ESHHKAKGK
Sequence of entity 5 (H, M), FASTA
>9EOZ_5 Histone H2B type 1-C/E/F/G/I (chains H, M)
PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMG
IMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTK
YTSSK
Sequence of entity 6 (Y), FASTA
>9EOZ_6 Widom 601 DNA (145-MER) (chains Y)
ATCAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAA
CGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAG
GCACGTGTCAGATATATACATCGAT
Sequence of entity 7 (Z), FASTA
>9EOZ_7 Widom 601 DNA (145-MER) (chains Z)
ATCGATGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCTTGGCGGTTAAA
ACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTACGACCAATTGA
GCGGCCTCGGCACCGGGATTCTGAT
Primary citation
Structural basis for human OGG1 processing 8-oxodGuo within nucleosome core particles. Ren, M., Gut, F., Fan, Y. et al. Nat Commun (2024) 15:9407-9407. DOI 10.1038/s41467-024-53811-3 · PubMed
Other PDB entries of the same protein (UniProt O15527 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8XWC 1.45 Å, Crystal structure of human 8-oxoguanine glycosylase K249H mutant bound to the substrate…
- 2XHI 1.55 Å, Separation-of-function mutants unravel the dual reaction mode of human 8-oxoguanine DNA…
- 5AN4 1.6 Å, Crystal structure of the human 8-oxoguanine glycosylase (OGG1) processed with the…
- 8XWU 1.68 Å, Crystal structure of human 8-oxoguanine glycosylase K249H mutant bound to the reaction…
- 8XXK 1.7 Å, Crystal structure of human 8-oxoguanine glycosylase K249H mutant bound to the reaction…
- 8XXG 1.82 Å, Crystal structure of human 8-oxoguanine glycosylase K249H mutant bound to the reaction…
- 9NZ8 1.85 Å, Crystal structure of human OGG1 in a DNA-free state
- 1M3Q 1.9 Å, Crystal Structure of hogg1 D268E Mutant with Base-Excised DNA and 8-aminoguanine
- 6RLW 2.0 Å, Structure of the human 8-oxoguanine DNA Glycosylase hOGG1 in complex with inhibitor TH5487
- 7AYY 2.0 Å, Structure of the human 8-oxoguanine DNA Glycosylase hOGG1 in complex with activator…
- 9NZ9 2.0 Å, Crystal structure of product-bound human OGG1(WT)
- 1LWY 2.01 Å, hOgg1 Borohydride-Trapped Intermediate without 8-oxoguanine
Browse structure collections
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