MolNFT v1 · #125900 · protein + RNA
Structure of bacterial 30S-IF3-mRNA-tRNA translation pre-initiation complex, closed form (state-4)
5LMU · 16S ribosomal RNA: “Structure of bacterial 30S-IF3-mRNA-tRNA translation pre-initiation complex, closed form (state-4)”. Electron microscopy, 2 ligands (MG, ZN), 20 pockets (best druggability 0.86). MolNFT v1 #125900 on GenesisL1…
- PDB
- 5LMU
- Type
- protein + RNA
- Length
- 4,162 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 16S ribosomal RNA; 30S ribosomal protein S2; 30S ribosomal protein S3; 30S ribosomal…
- UniProt
- P80371, P80372, P80373, Q5SHQ5, Q5SLP8, P17291, Q5SHQ2, P80374, Q5SHN7, P80376, Q5SHN3, P80377, Q5SHQ1, Q5SJ76, Q5SJH3, Q5SHP7, Q5SLQ0, Q5SHP2, P80380, Q5SIH3, Q5SKU2
- Ligands
- MG, ZN
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 24 distinct chains · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 16S ribosomal RNA | rna | 1515 | — | — |
| B | 30S ribosomal protein S2 | protein | 234 | 35% helix, 7% strand | P80371 |
| C | 30S ribosomal protein S3 | protein | 206 | 33% helix, 27% strand | P80372 |
| D | 30S ribosomal protein S4 | protein | 208 | 39% helix, 10% strand | P80373 |
| E | 30S ribosomal protein S5 | protein | 150 | 30% helix, 40% strand | Q5SHQ5 |
| F | 30S ribosomal protein S6 | protein | 101 | 31% helix, 49% strand | Q5SLP8 |
| G | 30S ribosomal protein S7 | protein | 155 | 57% helix, 10% strand | P17291 |
| H | 30S ribosomal protein S8 | protein | 138 | 28% helix, 30% strand | Q5SHQ2 |
| I | 30S ribosomal protein S9 | protein | 127 | 28% helix, 25% strand | P80374 |
| J | 30S ribosomal protein S10 | protein | 98 | 22% helix, 37% strand | Q5SHN7 |
| K | 30S ribosomal protein S11 | protein | 119 | 28% helix, 28% strand | P80376 |
| L | 30S ribosomal protein S12 | protein | 124 | 8% helix, 27% strand | Q5SHN3 |
| M | 30S ribosomal protein S13 | protein | 118 | 51% helix, 0% strand | P80377 |
| N | 30S ribosomal protein S14 type Z | protein | 60 | 13% helix, 5% strand | Q5SHQ1 |
| O | 30S ribosomal protein S15 | protein | 88 | 75% helix, 0% strand | Q5SJ76 |
| P | 30S ribosomal protein S16 | protein | 83 | 24% helix, 33% strand | Q5SJH3 |
| Q | 30S ribosomal protein S17 | protein | 99 | 17% helix, 46% strand | Q5SHP7 |
| R | 30S ribosomal protein S18 | protein | 73 | 34% helix, 7% strand | Q5SLQ0 |
| S | 30S ribosomal protein S19 | protein | 82 | 4% helix, 18% strand | Q5SHP2 |
| T | 30S ribosomal protein S20 | protein | 99 | 71% helix, 0% strand | P80380 |
| V | 30S ribosomal protein thx | protein | 24 | 25% helix, 0% strand | Q5SIH3 |
| X | Translation initiation factor if-3 | protein | 164 | 36% helix, 27% strand | Q5SKU2 |
| Y | MRNA | rna | 20 | — | — |
| Z | Trnai | rna | 77 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 80 copies · chains A, Q, K, P, E, L, Z
- ZN · Zinc ion · metal · 2 copies · chains D, N
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 827 | 0.86 | 0.90 | 72 | MG |
| 2 | 776 | 0.86 | 0.90 | 66 | empty |
| 3 | 644 | 0.86 | 0.91 | 73 | MG |
| 4 | 737 | 0.85 | 0.90 | 73 | MG |
| 5 | 895 | 0.84 | 0.87 | 69 | empty |
Interfaces
53 interfaces between chains.
- A–L · 3581 Ų buried · 92 hydrogen bonds · protein-nucleic
- A–D · 3393 Ų buried · 97 hydrogen bonds · protein-nucleic
- A–I · 3151 Ų buried · 76 hydrogen bonds · protein-nucleic
- A–T · 2883 Ų buried · 78 hydrogen bonds · protein-nucleic
- A–Q · 2847 Ų buried · 55 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 5 modified (nucleotide modification).
Compared structures
- 5LMU · Structure of bacterial 30S-IF3-mRNA-tRNA translation pre-initiation complex, closed form… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P80371
- Every structure of UniProt P80372
- Every structure of UniProt P80373
- Every structure of UniProt Q5SHQ5
- Every structure of UniProt Q5SLP8
- Every structure of UniProt P17291
- Every structure of UniProt Q5SHQ2
- Every structure of UniProt P80374
- Every structure of UniProt Q5SHN7
- Every structure of UniProt P80376
- Every structure of UniProt Q5SHN3
- Every structure of UniProt P80377
- Every structure of UniProt Q5SHQ1
- Every structure of UniProt Q5SJ76
- Every structure of UniProt Q5SJH3
- Every structure of UniProt Q5SHP7
- Every structure of UniProt Q5SLQ0
- Every structure of UniProt Q5SHP2
- Every structure of UniProt P80380
- Every structure of UniProt Q5SIH3
- Every structure of UniProt Q5SKU2
- Elsewhere: RCSB PDB 5LMU · PDBe 5LMU · UniProt P80371 · UniProt P80372 · UniProt P80373 · UniProt Q5SHQ5 · UniProt Q5SLP8 · UniProt P17291 · UniProt Q5SHQ2 · UniProt P80374 · UniProt Q5SHN7 · UniProt P80376 · UniProt Q5SHN3 · UniProt P80377 · UniProt Q5SHQ1 · UniProt Q5SJ76 · UniProt Q5SJH3 · UniProt Q5SHP7 · UniProt Q5SLQ0 · UniProt Q5SHP2 · UniProt P80380 · UniProt Q5SIH3 · UniProt Q5SKU2
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