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Crystal structure of a C-terminally truncated coccidioides posadasii mitochondrial tyrosyl-tRNA synthetase

Analyse Crystal structure of a C-terminally truncated coccidioides posadasii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IJX
Type: protein
Length: 365 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine--tRNA ligase, mitochondrial
EC: 6.1.1.1
UniProt: C5P455
Ligands: TYR
Pockets: 5 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine--tRNA ligase, mitochondrial (EC 6.1.1.1)	protein	365	58% helix, 9% strand	C5P455

Ligands and binding sites

TYR · Tyrosine · ligand · chains A

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

Pockets

5 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	282	0.67	0.83	39	TYR
2	195	0.49	0.76	31	empty
3	59	0.39	0.80	17	empty
4	75	0.38	0.77	17	empty
5	56	0.28	0.74	12	empty

Modifications

Observed in the structure: 11 modified (engineered).

Compared structures

5IJX · Crystal Structure of a C-terminally truncated Coccidioides posadasii mitochondrial… · the same entry in another collection · chain A against A, TM-score 1.00

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 C5P455
Elsewhere: RCSB PDB 5IJX · PDBe 5IJX · UniProt C5P455

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