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Conserved hypothetical proteim (TTHB059) from thermo thermophilus HB8

Analyse Conserved hypothetical proteim (TTHB059) from thermo thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2EHW
Type
protein
Length
463 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein TTHB059
UniProt
Q53WA3
Pockets
7 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 79% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHypothetical protein TTHB059protein11582% helix, 0% strandQ53WA3
CHypothetical protein TTHB059protein11776% helix, 0% strandQ53WA3
DHypothetical protein TTHB059protein11680% helix, 0% strandQ53WA3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110130.760.7970empty
2820.330.7413empty
3650.330.7613empty
4630.290.7411empty
5660.290.738empty

Interfaces

5 interfaces between chains.

  • C–D · 736 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 732 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 267 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 85 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 63 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 2EHW · Conserved hypothetical proteim (TTHB059) from Thermo thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00

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