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Crystal structure of symerythrin from cyanophora paradoxa, reduced with dithionite

Analyse Crystal structure of symerythrin from cyanophora paradoxa, reduced with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3QHC
Type
protein
Length
358 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Symerythrin
UniProt
P48329
Ligands
FE
Pockets
3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSymerythrinprotein17979% helix, 0% strandP48329

Ligands and binding sites

  • FE · Fe (III) ion · metal · 6 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11230.550.8328empty
22040.540.7835empty
31590.420.7427empty

Interfaces

1 interface between chains.

  • A–B · 1249 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 3QHC · Crystal structure of Symerythrin from Cyanophora paradoxa, reduced with dithionite · the same entry in another collection · chain A against A, TM-score 1.00
  • P48329 · AlphaFold monomer V2.0 prediction for uncharacterized protein in peta-psam intergenic… · a predicted model of the same protein · chain A against A, TM-score 0.95

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