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Crystal structure of the titin M10-obscurin ig domain 1 complex

Analyse Crystal structure of the titin M10-obscurin ig domain 1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4C4K
Type
protein
Length
191 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Obscurin; Titin
EC
2.7.11.1
UniProt
Q5VST9, Q8WZ42
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 61% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
OObscurin (EC 2.7.11.1)protein943% helix, 59% strandQ5VST9
TTitin (EC 2.7.11.1)protein976% helix, 63% strandQ8WZ42

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 12 copies · chains O, T

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1690.330.7616empty

Interfaces

1 interface between chains.

  • O–T · 824 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 4C4K · Crystal structure of the titin M10-Obscurin Ig domain 1 complex · the same entry in another collection · chain O against O, TM-score 1.00

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