MolNFT v1 · #143064 · protein

Crystal structure of arginyl-TRNA_SYNTHETASE from neisseria gonorrhoeae in complex with arginine

6AO8 · Arginine--tRNA ligase: “Crystal structure of arginyl-TRNA_SYNTHETASE from neisseria gonorrhoeae in complex with arginine”. X-ray diffraction, 1 ligand (ARG), 7 pockets (best druggability 0.56). MolNFT v1 #143064 on GenesisL1: 3D…

PDB: 6AO8
Type: protein
Length: 569 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arginine--tRNA ligase
EC: 6.1.1.19
UniProt: A0A1D3F609
Ligands: ARG
Pockets: 7 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Arginine--tRNA ligase (EC 6.1.1.19)	protein	569	55% helix, 12% strand	A0A1D3F609

Ligands and binding sites

ARG · Arginine · ligand · chains A
GOL · Glycerol · additive · chains A

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

Pockets

7 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	210	0.56	0.79	34	ARG
2	125	0.53	0.81	14	empty
3	132	0.44	0.76	23	empty
4	66	0.42	0.81	16	empty
5	57	0.39	0.80	13	empty

Compared structures

6AO8 · Crystal structure of arginyl-tRNA_synthetase from Neisseria gonorrhoeae in complex with… · 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 A0A1D3F609
Elsewhere: RCSB PDB 6AO8 · PDBe 6AO8 · UniProt A0A1D3F609

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