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Cryo-EM structure of 197BP nucleosome aided by scfv

Analyse Cryo-EM structure of 197BP nucleosome aided by scfv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7K61
Type
protein + DNA
Length
1,616 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone H3.1; Histone H4; Histone H2A type 1-B/E; Histone H2B type 1-J; DNA (197-mer)…
UniProt
P68431, P62805, P04908, P06899
Pockets
20 · best druggability 0.79

Structure

electron microscopy · 7 distinct chains · 42% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, EHistone H3.1protein9765% helix, 4% strandP68431
B, FHistone H4protein8360% helix, 8% strandP62805
C, GHistone H2A type 1-B/Eprotein10955% helix, 6% strandP04908
D, HHistone H2B type 1-Jprotein9573% helix, 4% strandP06899
IDNA (197-mer)dna197——
JDNA (197-mer)dna197——
M, NSCFV20protein2275% helix, 52% strand—

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17200.790.8371empty
24560.760.8549empty
34320.750.8547empty
43720.710.8335empty
51330.700.9129empty

Interfaces

39 interfaces between chains.

  • I–J · 8867 Ų buried · 693 hydrogen bonds · nucleic-nucleic
  • G–H · 2588 Ų buried · 28 hydrogen bonds · protein-protein
  • C–D · 2578 Ų buried · 24 hydrogen bonds · protein-protein
  • E–F · 2567 Ų buried · 23 hydrogen bonds · protein-protein
  • A–B · 2560 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 7K61 · Cryo-EM structure of 197bp nucleosome aided by scFv · the same entry in another collection · chain N against N, TM-score 1.00

Analyse

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