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Crystal structure of the L protein of rhodobacter sphaeroides light- independent protochlorophyllide reductase (bchl) with mgadp bound: a homologue of the nitrogenase fe protein

Analyse Crystal structure of the L protein of rhodobacter sphaeroides light… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FWY
Type
protein
Length
536 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
EC
1.18.-.-
UniProt
Q9RFD6
Ligands
ADP, SF4, MG
Pockets
4 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLight-independent protochlorophyllide reductase iron-sulfur ATP-binding protein (EC 1.18.-.-)protein26843% helix, 16% strandQ9RFD6

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
  • SF4 · Iron/sulfur cluster · ligand · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17610.800.8494MG, ADP
22720.740.8751empty
3920.420.7919empty
4760.390.7823empty

Interfaces

1 interface between chains.

  • A–B · 1534 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 3FWY · Crystal structure of the L protein of Rhodobacter sphaeroides light-independent… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9RFD6 · AlphaFold monomer V2.0 prediction for light-independent protochlorophyllide reductase… · a predicted model of the same protein · chain B against A, TM-score 0.97

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