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Cryo-EM structure of ncp-6-4PP

Analyse Cryo-EM structure of ncp-6-4PP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6R93
Type
protein + DNA
Length
1,065 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Human alpha-satellite DNA (145-mer); Human alpha-satellite DNA (145-mer) with a 6-4PP at…
UniProt
P68431, P62805, P04908, P06899
Pockets
20 · best druggability 0.79

Structure

electron microscopy · 7 distinct chains · 61% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
IHuman alpha-satellite DNA (145-mer)dna145——
JHuman alpha-satellite DNA (145-mer) with a 6-4PP at positions 95-96dna145——
A, EHistone H3.1protein9967% helix, 4% strandP68431
B, FHistone H4protein8260% helix, 9% strandP62805
CHistone H2A type 1-B/Eprotein11153% helix, 6% strandP04908
D, HHistone H2B type 1-Jprotein9772% helix, 4% strandP06899
GHistone H2A type 1-B/Eprotein10855% helix, 6% strandP04908

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15060.790.8650empty
24630.770.8556empty
34720.740.8343empty
41490.710.9129empty
57290.710.7853empty

Interfaces

36 interfaces between chains.

  • I–J · 6343 Ų buried · 425 hydrogen bonds · nucleic-nucleic
  • E–F · 2595 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 2556 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 2547 Ų buried · 9 hydrogen bonds · protein-protein
  • G–H · 2546 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nucleotide modification).

Compared structures

  • 6R93 · Cryo-EM structure of NCP-6-4PP · the same entry in another collection · chain I against I, TM-score 1.00

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