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Crystal structure of light-dependent protochlorophyllide oxidoreductase from synechocystis sp. pcc 6803

Analyse Crystal structure of light-dependent protochlorophyllide oxidoreductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6L1G
Type
protein
Length
594 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Light-dependent protochlorophyllide reductase
EC
1.3.1.33
UniProt
Q59987
Ligands
NDP, SO4
Pockets
5 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALight-dependent protochlorophyllide reductase (EC 1.3.1.33)protein30146% helix, 15% strandQ59987
BLight-dependent protochlorophyllide reductase (EC 1.3.1.33)protein29346% helix, 15% strandQ59987

Ligands and binding sites

  • NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 4 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15170.770.8466NDP
25330.750.8257NDP
32010.560.7926empty
42100.490.7528empty
5500.290.7613empty

Interfaces

1 interface between chains.

  • A–B · 734 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 6L1G · Crystal structure of light-dependent protochlorophyllide oxidoreductase from… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q59987 · AlphaFold monomer V2.0 prediction for light-dependent protochlorophyllide reductase… · a predicted model of the same protein · chain B against A, TM-score 0.95

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