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Structure of essential protein from trypanosoma brucei

Analyse Structure of essential protein from trypanosoma brucei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3K80
Type
protein
Length
452 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Antibody; MP18 RNA editing complex protein
UniProt
Q38B90
Pockets
2 · best druggability 0.34

Structure

x-ray diffraction · 4 distinct chains · 10% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAntibodyprotein12412% helix, 50% strand—
BAntibodyprotein12410% helix, 48% strand—
DMP18 RNA editing complex proteinprotein10110% helix, 63% strandQ38B90
CMP18 RNA editing complex proteinprotein10310% helix, 58% strandQ38B90

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1720.340.7623empty
2630.280.7318empty

Interfaces

3 interfaces between chains.

  • D–C · 1051 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 762 Ų buried · 16 hydrogen bonds · protein-protein
  • B–D · 710 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3K80 · Structure of essential protein from Trypanosoma brucei · the same entry in another collection · chain A against A, TM-score 1.00

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