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NMR structure of Sp140 PHD finger cis conformer

Analyse NMR structure of Sp140 PHD finger cis conformer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2MD8
Type
protein
Length
56 residues
Chains
1
Method
solution nmr
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
NOT
Source
Homo sapiens
Molecule
Nuclear body protein SP140
UniProt
Q13342
Ligands
ZN

Structure

solution nmr · resolution NOT · 1 distinct chain · 32% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CNuclear body protein SP140protein5632% helix, 0% strandQ13342

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains C

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 2MD8 · NMR structure of SP140 phd finger cis conformer · the same entry in another collection · chain C against C, TM-score 1.00
  • Q13342 · AlphaFold monomer V2.0 prediction for nuclear body protein SP140 (Q13342) · a predicted model of the same protein · chain C against A, TM-score 0.34

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