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The LIN28B cold shock domain in complex with heptathymidine

Analyse The LIN28B cold shock domain in complex with heptathymidine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4A76
Type
protein + DNA
Length
368 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LIN28 cold shock domain; 5'-D(*TP*TP*TP*TP*TP*TP*TP)-3'
UniProt
B4F6I0
Pockets
3 · best druggability 0.77

Structure

x-ray diffraction · 6 distinct chains · 7% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALIN28 cold shock domainprotein867% helix, 58% strandB4F6I0
B, D5'-D(*TP*TP*TP*TP*TP*TP*TP)-3'dna7——
CLIN28 cold shock domainprotein857% helix, 59% strandB4F6I0
ELIN28 cold shock domainprotein877% helix, 54% strandB4F6I0
F, H5'-D(*TP*TP*TP*TP*TP*TP*TP)-3'dna4——
GLIN28 cold shock domainprotein887% helix, 55% strandB4F6I0

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111660.770.7996empty
21870.570.8133empty
32010.490.7624empty

Interfaces

17 interfaces between chains.

  • C–D · 864 Ų buried · 13 hydrogen bonds · protein-nucleic
  • A–B · 858 Ų buried · 15 hydrogen bonds · protein-nucleic
  • G–H · 550 Ų buried · 8 hydrogen bonds · protein-nucleic
  • E–F · 540 Ų buried · 5 hydrogen bonds · protein-nucleic
  • C–G · 359 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 4A76 · The Lin28b Cold shock domain in complex with heptathymidine · the same entry in another collection · chain A against A, TM-score 1.00

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