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Backbone 1H, 13C, and 15N chemical shift assignments for the catalytic domain of B. anthracis srtd

Analyse Backbone 1H, 13C, and 15N chemical shift assignments for the catalytic domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2LN7
Type
protein
Length
147 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lpxtg-site transpeptidase family protein
UniProt
Q81KD1
Pockets
2 · best druggability 0.69

Structure

solution nmr · 1 distinct chain · 5% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALpxtg-site transpeptidase family proteinprotein1475% helix, 44% strandQ81KD1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12990.690.8333empty
21150.530.8224empty

Compared structures

  • 2LN7 · Backbone 1H, 13C, and 15N Chemical Shift Assignments for the catalytic domain of B.… · the same entry in another collection · chain A against A, TM-score 1.00

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