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Structure of functionally activated small ribosomal subunit at 3.3 a resolution

Analyse Structure of functionally activated small ribosomal subunit at 3.3 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FKA
Type
protein + RNA
Length
3,343 residues
Chains
20
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
16S ribosomal RNA; 30S ribosomal protein S2; 30S ribosomal protein S3; 30S ribosomal…
UniProt
P80373, P27152, P23370, P17291, P24319, P80378, P80381
Ligands
WO2
Pockets
20 · best druggability 0.82

Structure

x-ray diffraction · 19 distinct chains · 21% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A16S ribosomal RNArna1479——
B30S ribosomal protein S2protein1110% helix, 0% strand—
C30S ribosomal protein S3protein1760% helix, 0% strand—
D30S ribosomal protein S4protein16138% helix, 11% strandP80373
E30S ribosomal protein S5protein15719% helix, 25% strandP27152
F30S ribosomal protein S6protein9728% helix, 28% strandP23370
G30S ribosomal protein S7protein12859% helix, 2% strandP17291
H30S ribosomal protein S8protein13624% helix, 26% strandP24319
I30S ribosomal protein S9protein890% helix, 0% strand—
J, K30S ribosomal protein S10protein700% helix, 0% strand—
L30S ribosomal protein S12protein1030% helix, 0% strand—
M30S ribosomal protein S13protein770% helix, 0% strand—
N30S ribosomal protein S14protein260% helix, 0% strand—
O30S ribosomal protein S15protein8870% helix, 0% strandP80378
P30S ribosomal protein S16protein730% helix, 0% strand—
Q30S ribosomal protein S17protein8420% helix, 2% strand—
R30S ribosomal protein S18protein5022% helix, 0% strand—
S30S ribosomal protein S19protein7316% helix, 5% strandP80381
T30S ribosomal protein S20protein9553% helix, 0% strand—

Ligands and binding sites

  • WO2 · Octadecatungstenyl diphosphate · metal · 7 copies

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111220.820.84113empty
29210.810.8487empty
35760.810.8781empty
47210.800.8563empty
56970.790.8487empty

Interfaces

26 interfaces between chains.

  • A–H · 1080 Ų buried · 8 hydrogen bonds · protein-nucleic
  • A–O · 957 Ų buried · 12 hydrogen bonds · protein-nucleic
  • A–T · 861 Ų buried · 3 hydrogen bonds · protein-nucleic
  • A–I · 851 Ų buried · 0 hydrogen bonds · protein-nucleic
  • A–P · 773 Ų buried · 0 hydrogen bonds · protein-nucleic

Compared structures

  • 1FKA · Structure of functionally activated small ribosomal subunit at 3.3 a resolution · the same entry in another collection · chain H against H, TM-score 1.00

Analyse

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