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The structure of the moss psi-lhci reveals the evolution of the lhci antenna

Analyse The structure of the moss psi-lhci reveals the evolution of the lhci antenna in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KSQ
Type
protein
Length
3,347 residues
Chains
18
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Photosystem I P700 chlorophyll a apoprotein A1; Photosystem I P700 chlorophyll a…
EC
1.97.1.12
UniProt
Q8MFA3, Q8MFA2, A9T399, A0A2K1IW94, A9TEM8, A9RW10, Q6YXQ2, A9REG3, A9SPD7, A0A2K1IN36, A9SJ10, A9TCU9, Q6YXR3, Q6YXM2, A0A2K1JLW2, A9S1E1, Q6YXK4, A0A2K1JDE1
Ligands
CLA, BCR, CHL, LUT, LHG, LMG, SF4, PQN, CL0, DGD
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 18 distinct chains · 50% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhotosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12)protein74259% helix, 4% strandQ8MFA3
BPhotosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12)protein73258% helix, 2% strandQ8MFA2
1Chlorophyll a-B binding protein, chloroplasticprotein19247% helix, 2% strandA9T399
2Chlorophyll a-B binding protein, chloroplasticprotein20351% helix, 2% strandA0A2K1IW94
3Chlorophyll a-B binding protein, chloroplasticprotein21843% helix, 1% strandA9TEM8
4Chlorophyll a-B binding protein, chloroplasticprotein20345% helix, 1% strandA9RW10
CPhotosystem I iron-sulfur center (EC 1.97.1.12)protein8014% helix, 20% strandQ6YXQ2
DPsadprotein14215% helix, 25% strandA9REG3
EPsaeprotein635% helix, 37% strandA9SPD7
FPsi-Fprotein16055% helix, 5% strandA0A2K1IN36
GPsi-Gprotein9164% helix, 4% strandA9SJ10
HPsahprotein8739% helix, 1% strandA9TCU9
IPhotosystem I reaction center subunit VIIIprotein3471% helix, 0% strandQ6YXR3
JPhotosystem I reaction center subunit IXprotein4166% helix, 2% strandQ6YXM2
KPsakprotein8153% helix, 10% strandA0A2K1JLW2
LPsi subunit Vprotein16046% helix, 6% strandA9S1E1
MPhotosystem I reaction center subunit XIIprotein3087% helix, 0% strandQ6YXK4
OPsaoprotein8845% helix, 0% strandA0A2K1JDE1

Ligands and binding sites

  • CLA · Chlorophyll A · ligand · 144 copies · chains A, B, F, J, 3, K, O, D, H, L, I, M, G, 1, 4, 2
  • BCR · Beta-carotene · ligand · 27 copies · chains A, K, O, B, G, F, 1, 3, I, L, J, H, M
  • CHL · Chlorophyll B · ligand · 14 copies · chains B, 1, 4, 2, 3
  • LUT · (3R,3'R,6S)-4,5-didehydro-5,6-dihydro-beta,beta-carotene-3,3'-diol · ligand · 10 copies · chains 1, 2, 3, 4, F
  • LHG · 1,2-dipalmitoyl-phosphatidyl-glycerole · ligand · 7 copies · chains A, B, 1, 4, 2, 3
  • LMG · 1,2-distearoyl-monogalactosyl-diglyceride · ligand · 4 copies · chains A, 2, J, B, F
  • SF4 · Iron/sulfur cluster · ligand · 3 copies · chains A, B, C
  • PQN · Phylloquinone · ligand · 2 copies · chains A, J, B
  • CL0 · Chlorophyll A isomer · ligand · chains A, B
  • DGD · Digalactosyl diacyl glycerol (dgdg) · ligand · chains B, C
  • LMT · Dodecyl-beta-D-maltoside · additive · 6 copies · chains A, J, B, 1, G, 4, F

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
17760.840.8667CL0, CLA
28390.800.8381DGD
34480.780.8642CL0, CLA
49630.750.78106CLA, LHG
54050.720.8348empty

Interfaces

42 interfaces between chains.

  • A–B · 3536 Ų buried · 46 hydrogen bonds · protein-protein
  • H–L · 2004 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 1555 Ų buried · 22 hydrogen bonds · protein-protein
  • B–G · 1297 Ų buried · 24 hydrogen bonds · protein-protein
  • A–F · 1246 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 7KSQ · The Structure of the moss PSI-LHCI reveals the evolution of the LHCI antenna · the same entry in another collection · chain O against O, TM-score 1.00

Analyse

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