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Structure of psii-M

Analyse Structure of psii-M in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NHO
Type
protein
Length
2,086 residues
Chains
15
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Photosystem II protein D1 1; Photosystem II CP47 reaction center protein; Photosystem II…
EC
1.10.3.9
UniProt
P0A444, Q8DIQ1, Q8DIF8, Q8CM25, Q8DIP0, Q8DIN9, Q8DJ43, Q8DJZ6, Q9F1K9, Q8DIN8, Q8DHA7, Q8DIQ0, Q9F1R6, Q8DJI1, Q8DHJ2
Ligands
CLA, BCR, LMG, PHO, LHG, BCT, PL9, HEM, FE, MN, CL
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 15 distinct chains · 55% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhotosystem II protein D1 1 (EC 1.10.3.9)protein33558% helix, 4% strandP0A444
BPhotosystem II CP47 reaction center proteinprotein48545% helix, 11% strandQ8DIQ1
CPhotosystem II CP43 reaction center proteinprotein44851% helix, 4% strandQ8DIF8
DPhotosystem II D2 protein (EC 1.10.3.9)protein34061% helix, 2% strandQ8CM25
ECytochrome B559 subunit alphaprotein7755% helix, 0% strandQ8DIP0
FCytochrome B559 subunit betaprotein3853% helix, 0% strandQ8DIN9
HPhotosystem II reaction center protein Hprotein6548% helix, 2% strandQ8DJ43
IPhotosystem II reaction center protein Iprotein3574% helix, 0% strandQ8DJZ6
KPhotosystem II reaction center protein Kprotein3765% helix, 0% strandQ9F1K9
LPhotosystem II reaction center protein Lprotein3759% helix, 3% strandQ8DIN8
MPhotosystem II reaction center protein Mprotein3476% helix, 0% strandQ8DHA7
TPhotosystem II reaction center protein Tprotein3067% helix, 0% strandQ8DIQ0
XPhotosystem II reaction center X proteinprotein3586% helix, 0% strandQ9F1R6
yPhotosystem II reaction center protein YCF12protein2864% helix, 0% strandQ8DJI1
ZPhotosystem II reaction center protein Zprotein6276% helix, 0% strandQ8DHJ2

Ligands and binding sites

  • CLA · Chlorophyll A · ligand · 35 copies · chains A, D, T, L, I, B, H, M, X, C, K, y, Z
  • BCR · Beta-carotene · ligand · 10 copies · chains A, I, B, M, C, K, Z, D, F, H, X, y
  • LMG · 1,2-distearoyl-monogalactosyl-diglyceride · ligand · 7 copies · chains A, B, D, L, M, C, K, Z, F, T, I
  • PHO · Pheophytin A · ligand · 2 copies · chains A, D
  • LHG · 1,2-dipalmitoyl-phosphatidyl-glycerole · ligand · 2 copies · chains A, C, D
  • BCT · Bicarbonate ion · ligand · chains A, D
  • PL9 · 2,3-dimethyl-5-(3,7,11,15,19,23,27,31,35-nonamethyl-2, 6,10,14,18,22,26,30,34-hexatriacontanonaenyl-2,5-cyclohexadiene-1,4-dione-2,3-dimethyl-5-solanesyl-1,4-benzoquinone · ligand · chains A, D, L, T
  • HEM · Protoporphyrin IX containing Fe · ligand · chains E, F
  • FE · Fe (III) ion · metal · chains A, D
  • MN · Manganese (II) ion · metal · chains A
  • CL · Chloride ion · ion · chains A, D

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

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110950.840.8477CLA, BCR
28780.830.8597LMG
310690.820.83121MN, CL
411210.800.81109CLA
511060.780.7981CLA

Interfaces

36 interfaces between chains.

  • A–D · 5530 Ų buried · 47 hydrogen bonds · protein-protein
  • A–C · 3046 Ų buried · 20 hydrogen bonds · protein-protein
  • B–D · 2637 Ų buried · 23 hydrogen bonds · protein-protein
  • B–H · 2038 Ų buried · 18 hydrogen bonds · protein-protein
  • D–E · 1290 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 7NHO · Structure of PSII-M · the same entry in another collection · chain L against L, TM-score 1.00

Analyse

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