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Crystal structure of the regulatory domain of mtbglnr

Analyse Crystal structure of the regulatory domain of mtbglnr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4O1I
Type
protein
Length
566 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcriptional regulatory protein
UniProt
O53830
Pockets
3 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, ETranscriptional regulatory proteinprotein11335% helix, 22% strandO53830
DTranscriptional regulatory proteinprotein11435% helix, 21% strandO53830

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12790.600.7950empty
21200.440.7720empty
3700.360.7720empty

Interfaces

6 interfaces between chains.

  • C–D · 774 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 751 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 421 Ų buried · 1 hydrogen bond · protein-protein
  • C–E · 237 Ų buried · 0 hydrogen bonds · protein-protein
  • D–E · 111 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4O1I · Crystal Structure of the regulatory domain of MtbGlnR · the same entry in another collection · chain A against A, TM-score 1.00

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