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Crystal structure of octameric state of C-phycocyanin from thermoleptolyngbya sp. O-77

Analyse Crystal structure of octameric state of C-phycocyanin from thermoleptolyngbya… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EFV
Type
protein
Length
668 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
C-phycocyanin alpha chain; C-phycocyanin beta chain
UniProt
A0A0X8WU90, A0A0X8WUE0
Ligands
CYC
Pockets
11 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CC-phycocyanin alpha chainprotein16277% helix, 0% strandA0A0X8WU90
B, DC-phycocyanin beta chainprotein17276% helix, 0% strandA0A0X8WUE0

Ligands and binding sites

  • CYC · Phycocyanobilin · ligand · 6 copies · chains A, B, C, D

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

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17970.710.7770empty
2830.610.8819CYC
3770.590.8822CYC
41710.590.8230CYC
51620.580.8228CYC

Interfaces

5 interfaces between chains.

  • A–B · 1619 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 1601 Ų buried · 17 hydrogen bonds · protein-protein
  • A–C · 587 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 130 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 120 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 cofactor, 2 modified (phycocyanobilin attachment, nonstandard).

Compared structures

  • 7EFV · Crystal structure of octameric state of C-phycocyanin from Thermoleptolyngbya sp. O-77 · the same entry in another collection · chain A against A, TM-score 1.00

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