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Crystal structure of the acetyltransferase from agrobacterium tumefaciens str. C58

Analyse Crystal structure of the acetyltransferase from agrobacterium tumefaciens str.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FSR
Type
protein
Length
171 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acetyltransferase
UniProt
Q8UCP8
Pockets
2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetyltransferaseprotein17136% helix, 23% strandQ8UCP8

Ligands and binding sites

  • FMT · Formic acid · additive · chains A
  • PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13070.670.8232empty
21510.520.7924empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

  • 2FSR · Crystal Structure of the Acetyltransferase from Agrobacterium tumefaciens str. C58 · the same entry in another collection · chain A against A, TM-score 1.00

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