MolNFT v1 · #143516 · protein

Crystal structure of glutamate-tRNA synthetase from elizabethkingia anophelis

6B1Z · Glutamate--tRNA ligase: “Crystal structure of glutamate-tRNA synthetase from elizabethkingia anophelis”. X-ray diffraction, 1 ligand (MG), 6 pockets (best druggability 0.65). MolNFT v1 #143516 on GenesisL1: 3D structure, binding…

PDB: 6B1Z
Type: protein
Length: 495 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate--tRNA ligase
EC: 6.1.1.17
UniProt: A0A1T3FQP0
Ligands: MG
Pockets: 6 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate--tRNA ligase (EC 6.1.1.17)	protein	495	48% helix, 12% strand	A0A1T3FQP0

Ligands and binding sites

MG · Magnesium ion · metal · chains A
FMT · Formic acid · additive · 16 copies · chains A
EDO · 1,2-ethanediol · additive · 7 copies · chains A

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

Pockets

6 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	338	0.65	0.80	39	FMT
2	90	0.55	0.85	27	empty
3	128	0.36	0.72	25	FMT
4	66	0.34	0.76	13	empty
5	71	0.33	0.75	18	empty

Compared structures

6B1Z · Crystal Structure of Glutamate-tRNA Synthetase from Elizabethkingia anophelis · 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 A0A1T3FQP0
Elsewhere: RCSB PDB 6B1Z · PDBe 6B1Z · UniProt A0A1T3FQP0

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.