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Crystal structure of a tryptophanyl-tRNA synthetase from neisseria gonorrhoeae, apo

Analyse Crystal structure of a tryptophanyl-tRNA synthetase from neisseria gonorrhoeae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TEV
Type: protein
Length: 667 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tryptophan--tRNA ligase
EC: 6.1.1.2
UniProt: Q5F7X0
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tryptophan--tRNA ligase (EC 6.1.1.2)	protein	332	58% helix, 8% strand	Q5F7X0
B	Tryptophan--tRNA ligase (EC 6.1.1.2)	protein	335	58% helix, 9% strand	Q5F7X0

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	954	0.72	0.76	93	empty
2	762	0.71	0.77	67	empty
3	53	0.29	0.75	14	empty
4	54	0.28	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 199 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5TEV · Crystal structure of a tryptophanyl-tRNA synthetase from Neisseria gonorrhoeae, apo · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5F7X0
Elsewhere: RCSB PDB 5TEV · PDBe 5TEV · UniProt Q5F7X0

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