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Crystal structure of the csid glutarate hydroxylase in complex with succinate

Analyse Crystal structure of the csid glutarate hydroxylase in complex with succinate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6HL9
Type
protein
Length
593 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein csid
UniProt
A0A1X3JCQ2
Ligands
FE2
Pockets
5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein csidprotein29927% helix, 28% strandA0A1X3JCQ2
BProtein csidprotein29428% helix, 30% strandA0A1X3JCQ2

Ligands and binding sites

  • FE2 · Fe (II) ion · metal · 2 copies · chains A, B
  • SIN · Succinic acid · additive · 2 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13970.760.8548FE2, SIN
23580.680.8149FE2, SIN
31430.440.7626empty
41300.390.7418empty
5860.350.7519empty

Interfaces

1 interface between chains.

  • A–B · 531 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 6HL9 · Crystal Structure of the CsiD Glutarate Hydroxylase in complex with Succinate · the same entry in another collection · chain A against A, TM-score 1.00

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