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Crystal structure of an H-nox protein from T. tengcongensis

Analyse Crystal structure of an H-nox protein from T. tengcongensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TF0
Type
protein
Length
374 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methyl-accepting chemotaxis protein
UniProt
Q8RBX6
Ligands
HEM, OXY
Pockets
3 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMethyl-accepting chemotaxis proteinprotein18649% helix, 21% strandQ8RBX6
BMethyl-accepting chemotaxis proteinprotein18849% helix, 21% strandQ8RBX6

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
  • OXY · Oxygen molecule · ion · 2 copies · chains A, B
  • ACT · Acetate ion · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12980.810.9135HEM, OXY, ACT
23210.810.9138HEM, OXY
35080.620.7555empty

Interfaces

1 interface between chains.

  • A–B · 275 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 3TF0 · Crystal structure of an H-NOX protein from T. tengcongensis · the same entry in another collection · chain A against A, TM-score 1.00

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