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Trimeric photosystem I from the high-light tolerant cyanobacteria cyanobacterium aponinum

Analyse Trimeric photosystem I from the high-light tolerant cyanobacteria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VPV
Type
protein
Length
6,753 residues
Chains
33
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
A0A2G3P9X3, K9Z2J7, A0A2G3PD04, A0A2G3PAQ0, A0A2G3PEU8, A0A2G3PEV5, K9Z9J3, A0A2G3PEV6, A0A2G3P6W6, A0A2G3P7D5, A0A2G3PA81
Ligands
CLA, BCR, SF4, PQN, LHG, CL0, LMG, SQD
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 11 distinct chains · 51% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, a, 1Photosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12)protein74159% helix, 5% strandA0A2G3P9X3
B, b, 2Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12)protein73757% helix, 2% strandK9Z2J7
C, c, 3Photosystem I iron-sulfur center (EC 1.97.1.12)protein8015% helix, 20% strandA0A2G3PD04
D, d, 4Photosystem I reaction center subunit IIprotein13912% helix, 26% strandA0A2G3PAQ0
E, e, 5Photosystem I reaction center subunit IVprotein680% helix, 32% strandA0A2G3PEU8
F, f, 6Psi-Fprotein14147% helix, 6% strandA0A2G3PEV5
I, i, 7Photosystem I reaction center subunit VIIIprotein3866% helix, 3% strandK9Z9J3
J, j, 8Photosystem I reaction center subunit IXprotein3972% helix, 3% strandA0A2G3PEV6
K, k, 9Photosystem I reaction center subunit psakprotein7859% helix, 0% strandA0A2G3P6W6
L, l, 0Photosystem I reaction center subunit XIprotein16045% helix, 2% strandA0A2G3P7D5
M, m, zPhotosystem I reaction center subunit XIIprotein3087% helix, 0% strandA0A2G3PA81

Ligands and binding sites

  • CLA · Chlorophyll A · ligand · 285 copies · chains A, B, J, K, L, I, b, F, m, M, 0, 9, i, l, a, j, k, 2, f, z, 7, 1, 8, 6
  • BCR · Beta-carotene · ligand · 69 copies · chains A, B, F, J, I, K, L, 0, M, a, b, f, j, i, k, l, m, 1, 2, 6, 8, 7, 9, z
  • SF4 · Iron/sulfur cluster · ligand · 9 copies · chains A, B, C, a, b, c, 1, 2, 3
  • PQN · Phylloquinone · ligand · 6 copies · chains A, J, B, a, j, b, 1, 8, 2
  • LHG · 1,2-dipalmitoyl-phosphatidyl-glycerole · ligand · 6 copies · chains A, E, a, e, 1, 5
  • CL0 · Chlorophyll A isomer · ligand · 3 copies · chains A, B, a, b, 1, 2
  • LMG · 1,2-distearoyl-monogalactosyl-diglyceride · ligand · 3 copies · chains B, b, 2
  • SQD · 1,2-di-O-acyl-3-O-[6-deoxy-6-sulfo-alpha-D-glucopyranosyl]-sn-glycerol · ligand · 3 copies · chains B, I, L, 0, b, i, l, 2, 7

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
111340.860.86100CL0, CLA
29550.860.8678CL0, CLA
37390.830.8674CL0, CLA
411330.820.82124CLA, BCR
59640.810.8291CLA, LMG

Interfaces

87 interfaces between chains.

  • a–b · 3507 Ų buried · 37 hydrogen bonds · protein-protein
  • A–B · 3507 Ų buried · 37 hydrogen bonds · protein-protein
  • 1–2 · 3506 Ų buried · 38 hydrogen bonds · protein-protein
  • 3–4 · 1649 Ų buried · 17 hydrogen bonds · protein-protein
  • c–d · 1644 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 6VPV · Trimeric Photosystem I from the High-Light Tolerant Cyanobacteria Cyanobacterium Aponinum · the same entry in another collection · chain B against B, TM-score 1.00

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