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Structural genomics, the crystal structure of the acetyl transferase, modifies N-terminal serine of 50S ribosomal subunit protein L7/L12 from salmonella typhimurium

Analyse Structural genomics, the crystal structure of the acetyl transferase, modifies… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Z9U
Type
protein
Length
348 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acetyl transferase
EC
2.3.1.-
UniProt
Q8ZPC0
Ligands
SO4
Pockets
3 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetyl transferase (EC 2.3.1.-)protein17235% helix, 38% strandQ8ZPC0
BAcetyl transferase (EC 2.3.1.-)protein17635% helix, 37% strandQ8ZPC0

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 8 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18320.730.7879empty
21660.580.8225empty
31760.560.8029SO4

Interfaces

1 interface between chains.

  • A–B · 903 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 1Z9U · Structural Genomics, The crystal structure of the acetyl transferase, modifies N-terminal… · the same entry in another collection · chain A against A, TM-score 1.00

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