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Tryptophanyl-tRNA synthetase from cryptosporidium parvum

Analyse Tryptophanyl-tRNA synthetase from cryptosporidium parvum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HV0
Type: protein
Length: 704 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tryptophanyl-tRNA synthetase
EC: 6.1.1.2
UniProt: Q5CYP8
Ligands: TRP
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tryptophanyl-tRNA synthetase (EC 6.1.1.2)	protein	352	55% helix, 11% strand	Q5CYP8

Ligands and binding sites

TRP · Tryptophan · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.75	0.98	24	empty
2	385	0.69	0.81	50	TRP
3	315	0.67	0.82	40	TRP
4	154	0.50	0.78	26	empty
5	143	0.48	0.78	28	empty

Interfaces

1 interface between chains.

A–B · 1386 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

3HV0 · Tryptophanyl-tRNA synthetase from Cryptosporidium parvum · 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 Q5CYP8
Elsewhere: RCSB PDB 3HV0 · PDBe 3HV0 · UniProt Q5CYP8

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