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CARSP2 and scaffolded phycoerythrin beta subunits from the phycobilisome of porphyridium purpureum

Analyse CARSP2 and scaffolded phycoerythrin beta subunits from the phycobilisome of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LIY
Type
protein
Length
435 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CARSP2; B-phycoerythrin beta chain
UniProt
A0A5J4YX67, P11393
Ligands
PEB
Pockets
7 · best druggability 0.76

Structure

electron microscopy · 2 distinct chains · 52% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACARSP2protein819% helix, 35% strandA0A5J4YX67
B, CB-phycoerythrin beta chainprotein17772% helix, 2% strandP11393

Ligands and binding sites

  • PEB · Phycoerythrobilin · ligand · 6 copies · chains A, B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13220.760.8744PEB
23070.730.8639PEB
34650.650.7851PEB
41170.530.8228PEB
51010.430.7818empty

Interfaces

3 interfaces between chains.

  • A–B · 1855 Ų buried · 19 hydrogen bonds · protein-protein
  • A–C · 1522 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 185 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 cofactor, 2 modified (phycoerythrobilin attachment, nonstandard).

Compared structures

  • 7LIY · CaRSP2 and scaffolded phycoerythrin beta subunits from the phycobilisome of Porphyridium… · the same entry in another collection · chain A against A, TM-score 1.00
  • P11393 · AlphaFold monomer V2.0 prediction for B-phycoerythrin beta chain (P11393) · a predicted model of the same protein · chain B against A, TM-score 0.81

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