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Crystal structure of ttnm, a FE(II)-alpha-ketoglutarate-dependent hydroxylase from the tautomycetin biosynthesis pathway in streptomyces griseochromogenes at 2 a.

Analyse Crystal structure of ttnm, a FE(II)-alpha-ketoglutarate-dependent hydroxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7N7V
Type
protein
Length
634 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Predicted hydroxylase
UniProt
C6ZCS6
Ligands
FE2, CL
Pockets
4 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APredicted hydroxylaseprotein32134% helix, 21% strandC6ZCS6
BPredicted hydroxylaseprotein31335% helix, 21% strandC6ZCS6

Ligands and binding sites

  • FE2 · Fe (II) ion · metal · 2 copies · chains A, B
  • CL · Chloride ion · ion · 3 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
12330.570.7935CL
22500.560.7834FE2, CL
3500.310.7714empty
4570.300.7515empty

Interfaces

1 interface between chains.

  • A–B · 685 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 7N7V · Crystal structure of TtnM, a Fe(II)-alpha-ketoglutarate-dependent hydroxylase from the… · the same entry in another collection · chain A against A, TM-score 1.00

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