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LR6 rod linker and scaffolded phycoerythrin beta subunits from the phycobilisome of porphyridium purpureum

Analyse LR6 rod linker and scaffolded phycoerythrin beta subunits from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LIZ
Type
protein
Length
469 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LR6; B-phycoerythrin beta chain
UniProt
A0A5J4YMI8, P11393
Ligands
PEB
Pockets
7 · best druggability 0.81

Structure

electron microscopy · 2 distinct chains · 51% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALR6protein11521% helix, 28% strandA0A5J4YMI8
B, CB-phycoerythrin beta chainprotein17771% 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13710.810.9048PEB
26820.780.8372PEB
310970.760.7979PEB
41000.450.7924empty
5760.400.7916empty

Interfaces

3 interfaces between chains.

  • A–B · 2609 Ų buried · 24 hydrogen bonds · protein-protein
  • A–C · 1538 Ų buried · 13 hydrogen bonds · protein-protein
  • B–C · 298 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 cofactor, 2 modified (phycoerythrobilin attachment, nonstandard).

Compared structures

  • 7LIZ · LR6 rod linker and scaffolded phycoerythrin beta subunits from the phycobilisome of… · 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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