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Kinetic and structural changes in hsmtphers, induced by pathogenic mutations in human FARS2

Analyse Kinetic and structural changes in hsmtphers, induced by pathogenic mutations in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MGW
Type
protein
Length
406 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylalanine--tRNA ligase, mitochondrial
EC
6.1.1.20
UniProt
O95363
Ligands
PHE
Pockets
3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhenylalanine--tRNA ligase, mitochondrial (EC 6.1.1.20)protein40632% helix, 27% strandO95363

Ligands and binding sites

  • PHE · Phenylalanine · ligand · 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
15250.690.7954PHE
2750.450.8120empty
31080.350.7417empty

Compared structures

  • 5MGW · Kinetic and Structural Changes in HsmtPheRS, Induced by Pathogenic Mutations in Human… · the same entry in another collection · chain A against A, TM-score 1.00
  • O95363 · AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase, mitochondrial (O95363) · a predicted model of the same protein · chain A against A, TM-score 1.00

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