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NMR structure of LYS48-linked di-ubiquitin using chemical shift perturbation data together with rdcs and 15N- relaxation data

Analyse NMR structure of LYS48-linked di-ubiquitin using chemical shift perturbation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2BGF
Type
protein
Length
152 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Di-ubiquitin
UniProt
P62988

Structure

solution nmr · 1 distinct chain · 24% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BDi-ubiquitinprotein7624% helix, 36% strandP62988

Interfaces

1 interface between chains.

  • A–B · 868 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 2BGF · NMR structure of Lys48-linked di-ubiquitin using chemical shift perturbation data… · the same entry in another collection · chain A against A, TM-score 1.00

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