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Ensemble refinement of the protein crystal structure of AT3G17210 from arabidopsis thaliana

Analyse Ensemble refinement of the protein crystal structure of AT3G17210 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Q3P
Type
protein
Length
103 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized protein AT3G17210
UniProt
Q0WKU8
Ligands
MG
Pockets
1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUncharacterized protein AT3G17210protein10334% helix, 28% strandQ0WKU8

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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1580.420.8113empty

Modifications

Observed in the structure: 1 modified (engineered).

Compared structures

  • 2Q3P · Ensemble refinement of the protein crystal structure of At3g17210 from Arabidopsis… · the same entry in another collection · chain A against A, TM-score 1.00

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