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Crystal structure of the selenocysteine synthase sela and trnasec complex

Analyse Crystal structure of the selenocysteine synthase sela and trnasec complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3W1K
Type
protein + RNA
Length
2,720 residues
Chains
10
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-seryl-TRNA(SEC) selenium transferase; Selenocysteine tRNA
EC
2.9.1.1
UniProt
O67140
Pockets
20 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EL-seryl-TRNA(SEC) selenium transferase (EC 2.9.1.1)protein45240% helix, 17% strandO67140
F, G, H, I, JSelenocysteine tRNArna92——

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1930.750.9624empty
27770.750.8144empty
310560.740.7858empty
410480.740.7858empty
510310.740.7855empty

Interfaces

17 interfaces between chains.

  • C–D · 4273 Ų buried · 74 hydrogen bonds · protein-protein
  • A–B · 4218 Ų buried · 78 hydrogen bonds · protein-protein
  • D–E · 1208 Ų buried · 32 hydrogen bonds · protein-protein
  • B–C · 1204 Ų buried · 34 hydrogen bonds · protein-protein
  • D–H · 677 Ų buried · 17 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 5 modified (cofactor).

Compared structures

  • 3W1K · Crystal structure of the selenocysteine synthase SelA and tRNASec complex · the same entry in another collection · chain J against J, TM-score 1.00
  • O67140 · AlphaFold monomer V2.0 prediction for L-seryl-TRNA(SEC) selenium transferase (O67140) · a predicted model of the same protein · chain A against A, TM-score 0.97

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