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Peridinin-chlorophyll a protein, high-salt form

Analyse Peridinin-chlorophyll a protein, high-salt form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2C9E
Type
protein
Length
317 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.1
Source
AMPHIDINIUM CARTERAE
Molecule
Peridinin-chlorophyll a protein
UniProt
O76183
Ligands
PID, CLA, DGD, MG
Pockets
4 · best druggability 0.72

Structure

x-ray diffraction · resolution 2.1 · 1 distinct chain · 76% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeridinin-chlorophyll a proteinprotein31776% helix, 0% strandO76183

Ligands and binding sites

  • PID · Peridinin · ligand · 6 copies · chains A
  • CLA · Chlorophyll A · ligand · 2 copies · chains A
  • DGD · Digalactosyl diacyl glycerol (dgdg) · sugar · 2 copies · chains A
  • MG · Magnesium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110560.720.7564CLA, PID, DGD
29350.710.7568PID
33390.570.7535PID
4520.300.7613empty

Compared structures

  • 2C9E · Peridinin-chlorophyll a protein, high-salt form · the same entry in another collection · chain A against A, TM-score 1.00

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