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Molecular basis for the ribosome functioning as a L-tryptophan sensor - cryo-EM structure of a tnac stalled E.COLI ribosome

Analyse Molecular basis for the ribosome functioning as a L-tryptophan sensor - cryo-EM… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4UY8
Type
protein + RNA
Length
6,515 residues
Chains
35
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
50S ribosomal protein L32; 50S ribosomal protein L33; 50S ribosomal protein L34; 50S…
UniProt
U5SG25, U5SML7, P0A7P5, W0KX84, X7QRM8, E1IXH4, V5UZV4, A4GWE7, E3PCX7, X7QS81, D6IEL8, X7QRP4, X7QU92, X7QBP9, D8BKG3, E7HV64, X7QR95, E1PGS6, P02413, D7XL00, X7QRM3, X7QRN2, X7R0V6, X7QXR5, W0L2B9, E1JB10, C6EGE8, W0L2N0, W0KYJ4, C3SME2, D7X2Z3, W0L301
Ligands
TRP, MG, ZN
Pockets
20 · best druggability 0.87

Structure

electron microscopy · 35 distinct chains · 24% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
050S ribosomal protein L32protein5618% helix, 18% strandU5SG25
150S ribosomal protein L33protein500% helix, 48% strandU5SML7
250S ribosomal protein L34protein4654% helix, 0% strandP0A7P5
350S ribosomal protein L35protein6427% helix, 3% strandW0KX84
450S ribosomal protein L36protein388% helix, 29% strandX7QRM8
550S ribosomal protein L10protein14836% helix, 3% strandE1IXH4
6Ribosomal L7 proteinprotein3037% helix, 0% strandV5UZV4
7Tryptophanaseprotein200% helix, 0% strandA4GWE7
850S ribosomal protein L25protein9422% helix, 43% strandE3PCX7
ARRNA-23S ribosomal RNArna2854——
BRRNA-5S ribosomal RNArna118——
C50S ribosomal protein L2protein2718% helix, 20% strandX7QS81
D50S ribosomal protein L3protein2097% helix, 25% strandD6IEL8
E50S ribosomal protein L4protein20131% helix, 4% strandX7QRP4
F50S ribosomal protein L5protein17736% helix, 16% strandX7QU92
G50S ribosomal protein L6protein17618% helix, 23% strandX7QBP9
HRibosomal protein L9protein5028% helix, 10% strandD8BKG3
I50S ribosomal protein L11protein14118% helix, 4% strandE7HV64
J50S ribosomal protein L13protein14232% helix, 14% strandX7QR95
K50S ribosomal protein L14protein1229% helix, 35% strandE1PGS6
L50S ribosomal protein L15protein14315% helix, 10% strandP02413
M50S ribosomal protein L16protein13620% helix, 21% strandD7XL00
N50S ribosomal protein L17protein12048% helix, 13% strandX7QRM3
O50S ribosomal protein L18protein11641% helix, 16% strandX7QRN2
P50S ribosomal protein L19protein11418% helix, 32% strandX7R0V6
Q50S ribosomal protein L20protein11776% helix, 0% strandX7QXR5
R50S ribosomal protein L21protein1030% helix, 54% strandW0L2B9
S50S ribosomal protein L22protein11029% helix, 32% strandE1JB10
T50S ribosomal protein L23protein9319% helix, 18% strandC6EGE8
U50S ribosomal protein L24protein1023% helix, 39% strandW0L2N0
VRNArna77——
W50S ribosomal protein L27protein790% helix, 10% strandW0KYJ4
X50S ribosomal protein L28protein7722% helix, 21% strandC3SME2
Y50S ribosomal protein L29protein6367% helix, 0% strandD7X2Z3
Z50S ribosomal protein L30protein5838% helix, 17% strandW0L301

Ligands and binding sites

  • TRP · Tryptophan · ligand · 2 copies · chains 7, A
  • MG · Magnesium ion · metal · 143 copies · chains 4, A, E, L, C, Q, R, D, 3, T, J, B, 8
  • ZN · Zinc ion · metal · chains 4

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
19340.870.9084MG
211370.870.89119MG
310780.870.8988MG
45410.850.9264MG
55550.840.9173empty

Interfaces

68 interfaces between chains.

  • A–C · 7194 Ų buried · 212 hydrogen bonds · protein-nucleic
  • A–D · 5014 Ų buried · 112 hydrogen bonds · protein-nucleic
  • A–L · 4479 Ų buried · 126 hydrogen bonds · protein-nucleic
  • A–E · 4215 Ų buried · 96 hydrogen bonds · protein-nucleic
  • A–Q · 4141 Ų buried · 110 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 3 disulfide, 1 modified (disulfide, nucleotide modification).

Compared structures

  • 4UY8 · Molecular basis for the ribosome functioning as a L-tryptophan sensor - Cryo-EM structure… · the same entry in another collection · chain 1 against 1, TM-score 1.00

Analyse

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