GL1X · GenesisL1 explorer

Research workbench

Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (RV1652) from mycobacterium tuberculosis at 1.58 a resolution

Analyse Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (RV1652) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NQT
Type
protein
Length
692 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-acetyl-gamma-glutamyl-phosphate reductase
EC
1.2.1.38
UniProt
P63562
Pockets
10 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AN-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38)protein34732% helix, 22% strandP63562
BN-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38)protein34532% helix, 22% strandP63562

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12790.610.7952empty
22840.590.7848empty
31610.590.8324empty
4840.400.7818empty
5950.400.7719empty

Interfaces

1 interface between chains.

  • A–B · 1772 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

  • 2NQT · Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from… · 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.