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Crystal structure of pathogenic mutants of human mitochodnrial phers

Analyse Crystal structure of pathogenic mutants of human mitochodnrial phers in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MGH
Type: protein
Length: 405 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 0.67

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phenylalanine--tRNA ligase, mitochondrial (EC 6.1.1.20)	protein	405	32% helix, 27% strand	O95363

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	443	0.67	0.79	53	PHE
2	62	0.41	0.81	14	empty
3	81	0.30	0.72	15	empty

Compared structures

5MGH · Crystal structure of pathogenic mutants of human mitochodnrial PheRS · 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 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O95363
Elsewhere: RCSB PDB 5MGH · PDBe 5MGH · UniProt O95363

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