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Quantitative assessment of chlorophyll types in cryo-EM maps of photosystem I acclimated to far-red light

Analyse Quantitative assessment of chlorophyll types in cryo-EM maps of photosystem I… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LX0
Type
protein
Length
6,774 residues
Chains
36
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
G6FME9, A0A2N6KXB6, G6FW50, G6FW99, G6FQU3, G6FMD3, A0A2N6MR25, G6FMD2, A0A2N6L446, G6FWT6, G6FSH2
Ligands
CLA, BCR, F6C, LMG, SF4, PQN, LHG, CL0, CA
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 12 distinct chains · 51% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
G, a, APhotosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12)protein75157% helix, 4% strandG6FME9
H, b, BPhotosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12)protein73958% helix, 3% strandA0A2N6KXB6
N, c, CPhotosystem I iron-sulfur center (EC 1.97.1.12)protein8016% helix, 21% strandG6FW50
O, d, DPhotosystem I protein psadprotein13912% helix, 26% strandG6FW99
P, e, EPhotosystem I reaction center subunit IVprotein620% helix, 34% strandG6FQU3
Q, f, FPhotosystem I reaction center protein psaf subunit IIIprotein13551% helix, 5% strandG6FMD3
R, i, IPhotosystem I subunit VIIIprotein4257% helix, 2% strandA0A2N6MR25
S, j, JPhotosystem I reaction centre subunit IX / psajprotein4356% helix, 0% strandG6FMD2
T, k, KPhotosystem I reaction center subunit psakprotein4450% helix, 0% strand—
U, l, LPsi subunit Vprotein16356% helix, 4% strandA0A2N6L446
V, m, MPhotosystem I reaction center subunit XIIprotein3174% helix, 0% strandG6FWT6
W, x, XPhotosystem one psaxprotein2952% helix, 0% strandG6FSH2

Ligands and binding sites

  • CLA · Chlorophyll A · ligand · 252 copies · chains G, H, R, Q, S, T, U, B, V, W, I, L, a, b, i, f, j, k, l, m, x, A, F, J, K, M, X
  • BCR · Beta-carotene · ligand · 60 copies · chains G, T, H, W, S, Q, R, U, l, V, a, k, b, x, j, f, i, L, m, A, K, B, X, J, F, I, M
  • F6C · Chlorophyll F · ligand · 15 copies · chains G, H, R, U, l, Q, S, a, b, i, L, f, j, A, B, I, F, J
  • LMG · 1,2-distearoyl-monogalactosyl-diglyceride · ligand · 12 copies · chains G, U, H, R, V, l, I, a, b, i, m, L, A, B, M
  • SF4 · Iron/sulfur cluster · ligand · 9 copies · chains G, H, N, a, b, c, A, B, C
  • PQN · Phylloquinone · ligand · 6 copies · chains G, S, H, a, j, b, A, J, B
  • LHG · 1,2-dipalmitoyl-phosphatidyl-glycerole · ligand · 6 copies · chains G, H, W, a, b, x, A, B, X
  • CL0 · Chlorophyll A isomer · ligand · 3 copies · chains G, H, a, b, A, B
  • CA · Calcium ion · metal · 3 copies · chains G, U, a, l, A, L
  • LMT · Dodecyl-beta-D-maltoside · additive · 6 copies · chains G, M, V, a, m, A

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
110750.860.8699CL0, CLA
211160.860.8699CL0, CLA
310950.850.8698CL0, CLA
46450.830.8776F6C, BCR
58080.780.8263LMG

Interfaces

99 interfaces between chains.

  • A–B · 3570 Ų buried · 39 hydrogen bonds · protein-protein
  • a–b · 3554 Ų buried · 39 hydrogen bonds · protein-protein
  • G–H · 3552 Ų buried · 39 hydrogen bonds · protein-protein
  • N–O · 1679 Ų buried · 22 hydrogen bonds · protein-protein
  • C–D · 1679 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 7LX0 · Quantitative assessment of chlorophyll types in cryo-EM maps of photosystem I acclimated… · the same entry in another collection · chain N against N, TM-score 1.00

Analyse

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