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Crystal structure of triosephosphate isomerase from rhipicephalus (boophilus) microplus.

Analyse Crystal structure of triosephosphate isomerase from rhipicephalus (boophilus)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TH6
Type
protein
Length
485 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Triosephosphate isomerase
EC
5.3.1.1
UniProt
A8B3A8
Pockets
4 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATriosephosphate isomerase (EC 5.3.1.1)protein24443% helix, 16% strandA8B3A8
BTriosephosphate isomerase (EC 5.3.1.1)protein24146% helix, 16% strandA8B3A8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1980.760.9826empty
2960.470.8123empty
31500.430.7529empty
4740.400.7920empty

Interfaces

1 interface between chains.

  • A–B · 1676 Ų buried · 33 hydrogen bonds · protein-protein

Compared structures

  • 3TH6 · Crystal structure of Triosephosphate isomerase from Rhipicephalus (Boophilus) microplus. · the same entry in another collection · chain A against A, TM-score 1.00

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