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Structure of rslov D109G

Analyse Structure of rslov D109G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OBZ
Type
protein
Length
1,049 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lov protein
UniProt
M1E1F8
Ligands
FMN, SPD, NA, CL
Pockets
13 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 47% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALov proteinprotein17647% helix, 21% strandM1E1F8
B, C, D, FLov proteinprotein17547% helix, 22% strandM1E1F8
ELov proteinprotein17347% helix, 21% strandM1E1F8

Ligands and binding sites

  • FMN · Flavin mononucleotide · ligand · 6 copies · chains A, B, C, D, E, F
  • SPD · Spermidine · ligand · 5 copies · chains A, B, E
  • NA · Sodium ion · metal · 3 copies · chains B, C, D
  • CL · Chloride ion · ion · 13 copies · chains A, B, C, D

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

Pockets

13 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11800.750.9123FMN
21960.750.9025FMN
31640.750.9223FMN
47790.740.7973FMN
51730.720.9024FMN

Interfaces

5 interfaces between chains.

  • B–C · 1064 Ų buried · 12 hydrogen bonds · protein-protein
  • A–D · 1053 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 479 Ų buried · 2 hydrogen bonds · protein-protein
  • D–F · 193 Ų buried · 0 hydrogen bonds · protein-protein
  • D–E · 129 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7OBZ · Structure of RsLOV D109G · the same entry in another collection · chain A against A, TM-score 1.00

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