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B-cylinder of Synechocystis PCC 6803 Phycobilisome, complex with OCP - local refinement

Analyse B-cylinder of Synechocystis PCC 6803 Phycobilisome, complex with OCP - local… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7SCB
Type
protein
Length
4,743 residues
Chains
29
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.5
Source
Synechocystis sp. PCC 6803 substr. Kazusa
Molecule
Allophycocyanin alpha chain; Allophycocyanin beta chain; Allophycocyanin subunit alpha-B…
EC
4.-.-.-
UniProt
Q01951, Q01952, P72870, P74551, Q01950, Q55544, P73093, P74102, P74135
Ligands
CYC, 45D
Pockets
20 · best druggability 0.91

Structure

electron microscopy · resolution 2.5 · 9 distinct chains · 59% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AA, AC, AH, AJ, AN, AP, AR, AU, AW, AYAllophycocyanin alpha chainprotein16078% helix, 0% strandQ01951
AB, AD, AF, AI, AL, AO, AQ, AS, AV, AX, AZAllophycocyanin beta chainprotein16176% helix, 0% strandQ01952
AEAllophycocyanin subunit alpha-Bprotein16076% helix, 0% strandP72870
AKAllophycocyanin subunit beta-18protein16975% helix, 0% strandP74551
BB, BCPhycobilisome 7.8 kDa linker polypeptide, allophycocyanin-associated, coreprotein6725% helix, 31% strandQ01950
BEPhycobiliprotein ApcE (EC 4.-.-.-)protein64750% helix, 3% strandQ55544
BGPhycobilisome rod-core linker polypeptide CpcGprotein5725% helix, 0% strandP73093
BHOrange carotenoid-binding proteinprotein16955% helix, 1% strandP74102
BISll1873 proteinprotein3633% helix, 0% strandP74135

Ligands and binding sites

  • CYC · Phycocyanobilin · ligand · 24 copies · chains AA, AF, AB, BE, AC, AD, BB, AE, AH, AL, AI, AJ, AK, AN, AS, BI, AO, AP, AQ, AR, BH, AU, AZ, AV, BC, AW, AX, AY
  • 45D · beta,beta-carotene-4,4'-dione · ligand · chains AR, BH

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19060.910.94125CYC, 45D
29830.890.91120CYC
310150.890.90129CYC
48400.890.9291CYC
58310.880.9184CYC

Interfaces

112 interfaces between chains.

  • AL–BE · 2458 Ų buried · 25 hydrogen bonds · protein-protein
  • AK–BE · 1797 Ų buried · 23 hydrogen bonds · protein-protein
  • AI–BE · 1615 Ų buried · 27 hydrogen bonds · protein-protein
  • AU–AV · 1594 Ų buried · 11 hydrogen bonds · protein-protein
  • AA–AB · 1587 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 cofactor (phycocyanobilin attachment).

Compared structures

  • Q01952 · AlphaFold monomer V2.0 prediction for allophycocyanin beta chain (Q01952) · a predicted model of the same protein · chain AI against A, TM-score 0.99
  • Q01951 · AlphaFold monomer V2.0 prediction for allophycocyanin alpha chain (Q01951) · a predicted model of the same protein · chain AA against A, TM-score 0.98
  • P74551 · AlphaFold monomer V2.0 prediction for allophycocyanin subunit beta-18 (P74551) · a predicted model of the same protein · chain AK against A, TM-score 0.97

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