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Cryo-EM structure of sulfur oxygenase reductase from sulfurisphaera tokodaii

Analyse Cryo-EM structure of sulfur oxygenase reductase from sulfurisphaera tokodaii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6M3X
Type
protein
Length
7,440 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sulfur OXYGENASE/REDUCTASE
EC
1.13.11.55
UniProt
Q972K4
Ligands
FE
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 36% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, XSulfur OXYGENASE/REDUCTASE (EC 1.13.11.55)protein31036% helix, 31% strandQ972K4

Ligands and binding sites

  • FE · Fe (III) ion · metal · 24 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X

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
17850.880.9160empty
27840.880.9160empty
37930.880.9160empty
47930.880.9060empty
57850.880.9060empty

Interfaces

72 interfaces between chains.

  • C–E · 2734 Ų buried · 55 hydrogen bonds · protein-protein
  • R–W · 2734 Ų buried · 55 hydrogen bonds · protein-protein
  • B–X · 2731 Ų buried · 55 hydrogen bonds · protein-protein
  • G–U · 2731 Ų buried · 55 hydrogen bonds · protein-protein
  • D–Q · 2730 Ų buried · 55 hydrogen bonds · protein-protein

Compared structures

  • 6M3X · Cryo-EM structure of sulfur oxygenase reductase from Sulfurisphaera tokodaii · the same entry in another collection · chain A against A, TM-score 1.00

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