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X-ray structure of the H225N mutant of TCAB9, a C-3'- methyltransferase, in complex with S-adenosyl-L-homocysteine and sugar product

Analyse X-ray structure of the H225N mutant of TCAB9, a C-3'- methyltransferase, in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4E2Z
Type
protein
Length
405 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TCAB9
EC
2.1.1.-
UniProt
B5L6K6
Ligands
SAH, JHZ, ZN
Pockets
3 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATCAB9 (EC 2.1.1.-)protein40538% helix, 24% strandB5L6K6

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · chains A
  • JHZ · (2R,4S,6R)-4-amino-4,6-dimethyl-5-oxotetrahydro-2H-pyran-2-yl [(2R,3S,5R)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl dihydrogen diphosphate (non-preferred name) · ligand · chains A
  • ZN · Zinc ion · metal · chains A
  • EDO · 1,2-ethanediol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14010.850.9359SAH, JHZ
2790.350.7614empty
3690.350.7720empty

Compared structures

  • 4E2Z · X-ray Structure of the H225N mutant of TcaB9, a C-3'-Methyltransferase, in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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