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Crystal structure of an N-acetyltransferase from helicobacter pullorum in the presence of coenzyme a and dtdp-3-acetamido-3,6-dideoxy-D- galactose

Analyse Crystal structure of an N-acetyltransferase from helicobacter pullorum in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7S42
Type
protein
Length
145 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-acetyltransferase
Ligands
87Z, COA, NA

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AN-acetyltransferaseprotein1450% helix, 30% strand—

Ligands and binding sites

  • 87Z · [(2~{R},3~{R},4~{S},5~{R},6~{R})-4-acetamido-6-methyl-3,5-bis(oxidanyl)oxan-2-yl] [[(2~{R},3~{S},5~{R})-5-[5-methyl-2,4-bis(oxidanylidene)pyrimidin-1-yl]-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] hydrogen phosphate · ligand · chains A
  • COA · Coenzyme A · ligand · chains A
  • NA · Sodium ion · metal · chains A
  • EDO · 1,2-ethanediol · additive · 6 copies · chains A

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

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 7S42 · Crystal structure of an N-acetyltransferase from Helicobacter pullorum in the presence of… · the same entry in another collection · chain A against A, TM-score 1.00

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