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Crystal structure of the cysteine desulfurase csda from escherichia COLI at 1.996 angstroem resolution

Analyse Crystal structure of the cysteine desulfurase csda from escherichia COLI at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5FT4
Type
protein
Length
798 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cysteine desulfurase csda
EC
2.8.1.7, 4.4.1.-, 4.4.1.16
UniProt
Q46925
Ligands
PLP
Pockets
4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCysteine desulfurase csda (EC 2.8.1.7, 4.4.1.-, 4.4.1.16)protein39943% helix, 17% strandQ46925

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
  • GOL · Glycerol · additive · 6 copies · chains A, B
  • CIT · Citric acid · additive · 4 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
111900.810.82174PLP, GOL, CIT
22220.610.8129GOL
3780.420.7920empty
4840.410.7819empty

Interfaces

1 interface between chains.

  • A–B · 3315 Ų buried · 38 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).

Compared structures

  • 5FT4 · Crystal structure of the cysteine desulfurase CsdA from Escherichia coli at 1.996… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q46925 · AlphaFold monomer V2.0 prediction for cysteine desulfurase csda (Q46925) · a predicted model of the same protein · chain B against A, TM-score 0.99

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