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Cryoem structure of arabidopsis thaliana phytochrome B

Analyse Cryoem structure of arabidopsis thaliana phytochrome B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RZW
Type
protein
Length
1,723 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phytochrome B
UniProt
P14713
Ligands
O6E
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 2 distinct chains · 37% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhytochrome Bprotein85936% helix, 23% strandP14713
BPhytochrome Bprotein86437% helix, 21% strandP14713

Ligands and binding sites

  • O6E · 3-[5-[[(3~{R},4~{R})-3-ethyl-4-methyl-5-oxidanylidene-3,4-dihydropyrrol-2-yl]methyl]-2-[[5-[(4-ethyl-3-methyl-5-oxidanylidene-pyrrol-2-yl)methyl]-3-(3-hydroxy-3-oxopropyl)-4-methyl-1~{H}-pyrrol-2-yl]methyl]-4-methyl-1~{H}-pyrrol-3-yl]propanoic acid · ligand · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13280.840.9444O6E
23990.810.8961O6E
310310.750.7876empty
410510.750.7783empty
54080.700.8151empty

Interfaces

1 interface between chains.

  • A–B · 5075 Ų buried · 33 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 7RZW · CryoEM structure of Arabidopsis thaliana phytochrome B · the same entry in another collection · chain A against A, TM-score 1.00
  • P14713 · AlphaFold monomer V2.0 prediction for phytochrome B (P14713) · a predicted model of the same protein · chain B against A, TM-score 0.60

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