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Structure of serum resistance associated protein from T. B. rhodesiense

Analyse Structure of serum resistance associated protein from T. B. rhodesiense in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ELU
Type
protein
Length
2,450 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serum resistance associated; G10_3 heavy chain; G10_3 light chain
UniProt
Q8T309
Pockets
20 · best druggability 0.78

Structure

x-ray diffraction · 6 distinct chains · 51% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerum resistance associatedprotein19378% helix, 0% strandQ8T309
B, E, H, KG10_3 heavy chainprotein2227% helix, 50% strand—
C, F, I, LG10_3 light chainprotein2176% helix, 54% strand—
DSerum resistance associatedprotein16179% helix, 0% strandQ8T309
GSerum resistance associatedprotein16881% helix, 0% strandQ8T309
JSerum resistance associatedprotein17280% helix, 0% strandQ8T309

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110430.780.80110empty
29410.780.8195empty
35310.610.7455empty
43060.590.7852empty
53930.560.7448empty

Interfaces

21 interfaces between chains.

  • K–L · 1959 Ų buried · 14 hydrogen bonds · protein-protein
  • H–I · 1936 Ų buried · 14 hydrogen bonds · protein-protein
  • E–F · 1924 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 1923 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 577 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide (disulfide).

Compared structures

  • 6ELU · Structure of Serum Resistance Associated protein from T. b. rhodesiense · the same entry in another collection · chain I against I, TM-score 1.00

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