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Crystal structure of first N-terminal utrophin spectrin repeat

Analyse Crystal structure of first N-terminal utrophin spectrin repeat in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3UUL
Type
protein
Length
232 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Utrophin
UniProt
O55147
Ligands
MG
Pockets
3 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 87% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUtrophinprotein11587% helix, 0% strandO55147
BUtrophinprotein11786% helix, 0% strandO55147

Ligands and binding sites

  • MG · Magnesium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12600.510.7527empty
21660.440.7518empty
3970.420.7816empty

Interfaces

1 interface between chains.

  • A–B · 236 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 3UUL · Crystal Structure of first N-terminal utrophin spectrin repeat · the same entry in another collection · chain A against A, TM-score 1.00

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