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Crystal structure of neisseria gonorrhoeae leurs E169G mutant

Analyse Crystal structure of neisseria gonorrhoeae leurs E169G mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NU1
Type: protein
Length: 805 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Leucine--tRNA ligase
EC: 6.1.1.4
UniProt: B4RNT1
Ligands: ZN, MG
Pockets: 8 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Leucine--tRNA ligase (EC 6.1.1.4)	protein	805	42% helix, 19% strand	B4RNT1

Ligands and binding sites

ZN · Zinc ion · metal · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

8 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	821	0.76	0.80	85	empty
2	316	0.68	0.82	48	empty
3	66	0.49	0.85	15	empty
4	66	0.47	0.84	22	empty
5	130	0.43	0.76	27	empty

Compared structures

7NU1 · Crystal Structure of Neisseria gonorrhoeae LeuRS E169G mutant · the same entry in another collection · chain A against A, TM-score 1.00
B4RNT1 · AlphaFold monomer V2.0 prediction for leucine--tRNA ligase (B4RNT1) · a predicted model of the same protein · chain A against A, TM-score 0.98

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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 B4RNT1
Elsewhere: RCSB PDB 7NU1 · PDBe 7NU1 · UniProt B4RNT1

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