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Crystal structure of methionyl-tRNA formyltransferase from pseudomonas aeruginosa

Analyse Crystal structure of methionyl-tRNA formyltransferase from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5UAI
Type
protein
Length
1,243 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methionyl-tRNA formyltransferase
EC
2.1.2.9
UniProt
O85732
Pockets
5 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMethionyl-tRNA formyltransferase (EC 2.1.2.9)protein31027% helix, 28% strandO85732
B, C, DMethionyl-tRNA formyltransferase (EC 2.1.2.9)protein31128% helix, 28% strandO85732

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111240.850.86111empty
26920.800.8461empty
36430.790.8456empty
41120.390.7622empty
5910.330.7416empty

Interfaces

3 interfaces between chains.

  • A–B · 1225 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 1142 Ų buried · 7 hydrogen bonds · protein-protein
  • A–D · 250 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5UAI · Crystal structure of Methionyl-tRNA formyltransferase from Pseudomonas aeruginosa · the same entry in another collection · chain D against D, TM-score 1.00
  • O85732 · AlphaFold monomer V2.0 prediction for methionyl-tRNA formyltransferase (O85732) · a predicted model of the same protein · chain C against A, TM-score 0.98

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