GL1X · GenesisL1 explorer

Research workbench

Crystal structure of neisseria meningitidis earp bound tdp

Analyse Crystal structure of neisseria meningitidis earp bound tdp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7F2A
Type
protein
Length
752 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor P maturation arginine rhamnosyltransferase earp
UniProt
X5EQ00
Ligands
TYD, SO4
Pockets
6 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, FElongation factor P maturation arginine rhamnosyltransferase earpprotein37643% helix, 18% strandX5EQ00

Ligands and binding sites

  • TYD · Thymidine-5'-diphosphate · ligand · 2 copies · chains A, F
  • SO4 · Sulfate ion · ion · 4 copies · chains A, F

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110920.870.88126TYD
2620.700.9619empty
31660.630.8524empty
41240.600.8518empty
5630.430.8217empty

Interfaces

1 interface between chains.

  • A–F · 1007 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 7F2A · Crystal structure of Neisseria meningitidis EarP bound TDP · 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.