GL1X · GenesisL1 explorer

Research workbench

Crystal structure of a glutamine-dependent NAD(+) synthetase from cytophaga hutchinsonii

Analyse Crystal structure of a glutamine-dependent NAD(+) synthetase from cytophaga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ILV
Type
protein
Length
580 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamine-dependent NAD(+) synthetase
EC
6.3.5.1
UniProt
Q11SE1
Pockets
8 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamine-dependent NAD(+) synthetase (EC 6.3.5.1)protein58041% helix, 21% strandQ11SE1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13960.630.7847empty
21200.580.8520empty
3940.540.8420empty
42390.520.7634empty
5780.370.7713empty

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 3ILV · Crystal structure of a glutamine-dependent NAD(+) synthetase from Cytophaga hutchinsonii · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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