MolNFT v1 · #27541 · protein + RNA
Crystal structure of T6A37-asllysuuu aaa-mRNA bound to the decoding center
1XMQ · 16S ribosomal RNA: “Crystal structure of T6A37-asllysuuu aaa-mRNA bound to the decoding center”. X-ray diffraction, 3 ligands (PAR, MG, ZN), 20 pockets (best druggability 0.89). MolNFT v1 #27541 on GenesisL1: 3D structure, binding…
- PDB
- 1XMQ
- Type
- protein + RNA
- Length
- 3,918 residues
- Chains
- 23
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 16S ribosomal RNA; A-site messenger RNA; Anticodon RNA; 30S ribosomal protein S2; 30S…
- UniProt
- P80371, P80372, P80373, P27152, P23370, P17291, P62668, P80374, P80375, P80376, P80377, P24320, P80378, P80379, P62658, P80382, P80381, P80380, P62612
- Ligands
- PAR, MG, ZN
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 23 distinct chains · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 16S ribosomal RNA | rna | 1507 | — | — |
| W | A-site messenger RNA | rna | 4 | — | — |
| X | Anticodon RNA | rna | 11 | — | — |
| B | 30S ribosomal protein S2 | protein | 234 | 41% helix, 9% strand | P80371 |
| C | 30S ribosomal protein S3 | protein | 206 | 33% helix, 15% strand | P80372 |
| D | 30S ribosomal protein S4 | protein | 208 | 40% helix, 8% strand | P80373 |
| E | 30S ribosomal protein S5 | protein | 150 | 29% helix, 38% strand | P27152 |
| F | 30S ribosomal protein S6 | protein | 101 | 29% helix, 36% strand | P23370 |
| G | 30S ribosomal protein S7 | protein | 155 | 55% helix, 9% strand | P17291 |
| H | 30S ribosomal protein S8 | protein | 138 | 29% helix, 30% strand | P62668 |
| I | 30S ribosomal protein S9 | protein | 127 | 32% helix, 20% strand | P80374 |
| J | 30S ribosomal protein S10 | protein | 98 | 9% helix, 21% strand | P80375 |
| K | 30S ribosomal protein S11 | protein | 119 | 27% helix, 30% strand | P80376 |
| L | 30S ribosomal protein S12 | protein | 124 | 6% helix, 23% strand | — |
| M | 30S ribosomal protein S13 | protein | 125 | 45% helix, 2% strand | P80377 |
| N | 30S ribosomal protein S14 | protein | 60 | 22% helix, 7% strand | P24320 |
| O | 30S ribosomal protein S15 | protein | 88 | 73% helix, 0% strand | P80378 |
| P | 30S ribosomal protein S16 | protein | 83 | 22% helix, 29% strand | P80379 |
| Q | 30S ribosomal protein S17 | protein | 104 | 13% helix, 47% strand | P62658 |
| R | 30S ribosomal protein S18 | protein | 73 | 38% helix, 8% strand | P80382 |
| S | 30S ribosomal protein S19 | protein | 80 | 23% helix, 16% strand | P80381 |
| T | 30S ribosomal protein S20 | protein | 99 | 67% helix, 0% strand | P80380 |
| V | 30S ribosomal protein thx | protein | 24 | 25% helix, 8% strand | P62612 |
Ligands and binding sites
- PAR · Paromomycin · ligand · chains A
- MG · Magnesium ion · metal · 107 copies · chains A, E, N, V, L, T, W, J, P, X
- ZN · Zinc ion · metal · 2 copies · chains D, A, 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 | 1052 | 0.89 | 0.91 | 99 | MG |
| 2 | 1100 | 0.86 | 0.88 | 97 | MG |
| 3 | 763 | 0.85 | 0.89 | 94 | empty |
| 4 | 857 | 0.84 | 0.88 | 84 | MG |
| 5 | 1076 | 0.84 | 0.86 | 94 | MG |
Interfaces
48 interfaces between chains.
- A–L · 3312 Ų buried · 93 hydrogen bonds · protein-nucleic
- A–I · 3083 Ų buried · 101 hydrogen bonds · protein-nucleic
- A–D · 2837 Ų buried · 87 hydrogen bonds · protein-nucleic
- A–Q · 2768 Ų buried · 62 hydrogen bonds · protein-nucleic
- A–T · 2624 Ų buried · 66 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 1XMQ · Crystal Structure of t6A37-ASLLysUUU AAA-mRNA Bound to the Decoding Center · the same entry in another collection · chain I against I, 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 P27152
- Every structure of UniProt P23370
- Every structure of UniProt P17291
- Every structure of UniProt P62668
- Every structure of UniProt P80374
- Every structure of UniProt P80375
- Every structure of UniProt P80376
- Every structure of UniProt P80377
- Every structure of UniProt P24320
- Every structure of UniProt P80378
- Every structure of UniProt P80379
- Every structure of UniProt P62658
- Every structure of UniProt P80382
- Every structure of UniProt P80381
- Every structure of UniProt P80380
- Every structure of UniProt P62612
- Elsewhere: RCSB PDB 1XMQ · PDBe 1XMQ · UniProt P80371 · UniProt P80372 · UniProt P80373 · UniProt P27152 · UniProt P23370 · UniProt P17291 · UniProt P62668 · UniProt P80374 · UniProt P80375 · UniProt P80376 · UniProt P80377 · UniProt P24320 · UniProt P80378 · UniProt P80379 · UniProt P62658 · UniProt P80382 · UniProt P80381 · UniProt P80380 · UniProt P62612
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