MolNFT v1 · #153225 · protein

Crystal structure of central domain of fleq in complex with atpgs and mg

6J7E · Nitrogen assimilation regulatory protein: “Crystal structure of central domain of fleq in complex with atpgs and mg”. X-ray diffraction, 2 ligands (AGS, MG), 2 pockets (best druggability 0.57). MolNFT v1 #153225 on GenesisL1: 3D…

PDB: 6J7E
Type: protein
Length: 251 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitrogen assimilation regulatory protein
UniProt: Q51460
Ligands: AGS, MG
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitrogen assimilation regulatory protein	protein	251	45% helix, 16% strand	Q51460

Ligands and binding sites

AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	219	0.57	0.79	32	AGS, MG
2	69	0.40	0.79	15	empty

Compared structures

6J7E · Crystal Structure of Central domain of FleQ in complex with ATPgS and Mg · 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 Q51460
Elsewhere: RCSB PDB 6J7E · PDBe 6J7E · UniProt Q51460

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