MolNFT v1 · #189106 · protein + RNA
T.THERMOPHILUS 30S ribosome with ksga, class K1K4
7V2M · 16S ribosomal RNA: “T.THERMOPHILUS 30S ribosome with ksga, class K1K4”. Electron microscopy, 1 ligand (ZN), 20 pockets (best druggability 0.88). MolNFT v1 #189106 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7V2M
- Type
- protein + RNA
- Length
- 4,395 residues
- Chains
- 23
- 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…
- EC
- 2.1.1.182
- UniProt
- P80371, P80372, P80373, Q5SHQ5, Q5SLP8, P17291, P0DOY9, P80374, Q5SHN7, P80376, Q5SHN3, P80377, P0DOY6, Q5SJ76, Q5SJH3, P0DOY7, Q5SLQ0, Q5SHP2, P80380, P37468, Q5SIH3
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 23 distinct chains · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 16S ribosomal RNA | rna | 1486 | — | — |
| B | 30S ribosomal protein S2 | protein | 220 | 48% helix, 13% strand | P80371 |
| C | 30S ribosomal protein S3 | protein | 206 | 39% helix, 23% strand | P80372 |
| D | 30S ribosomal protein S4 | protein | 208 | 41% helix, 10% strand | P80373 |
| E | 30S ribosomal protein S5 | protein | 150 | 29% helix, 43% strand | Q5SHQ5 |
| F | 30S ribosomal protein S6 | protein | 101 | 24% helix, 44% strand | Q5SLP8 |
| G | 30S ribosomal protein S7 | protein | 155 | 55% helix, 6% strand | P17291 |
| H | 30S ribosomal protein S8 | protein | 138 | 28% helix, 30% strand | P0DOY9 |
| I | 30S ribosomal protein S9 | protein | 127 | 29% helix, 21% strand | P80374 |
| J | 30S ribosomal protein S10 | protein | 98 | 23% helix, 34% strand | Q5SHN7 |
| K | 30S ribosomal protein S11 | protein | 119 | 28% helix, 24% strand | P80376 |
| L | 30S ribosomal protein S12 | protein | 124 | 7% helix, 27% strand | Q5SHN3 |
| M | 30S ribosomal protein S13 | protein | 113 | 52% helix, 2% strand | P80377 |
| N | 30S ribosomal protein S14 type Z | protein | 60 | 27% helix, 12% strand | P0DOY6 |
| O | 30S ribosomal protein S15 | protein | 88 | 76% helix, 0% strand | Q5SJ76 |
| P | 30S ribosomal protein S16 | protein | 81 | 23% helix, 36% strand | Q5SJH3 |
| Q | 30S ribosomal protein S17 | protein | 100 | 17% helix, 49% strand | P0DOY7 |
| R | 30S ribosomal protein S18 | protein | 69 | 38% helix, 6% strand | Q5SLQ0 |
| S | 30S ribosomal protein S19 | protein | 80 | 24% helix, 19% strand | Q5SHP2 |
| T | 30S ribosomal protein S20 | protein | 99 | 73% helix, 0% strand | P80380 |
| U | Ribosomal RNA small subunit methyltransferase a (EC 2.1.1.182) | protein | 288 | 40% helix, 15% strand | P37468 |
| V | 30S ribosomal protein thx | protein | 24 | 29% helix, 0% strand | Q5SIH3 |
| W | Ribosomal RNA small subunit methyltransferase a (EC 2.1.1.182) | protein | 261 | 37% helix, 17% strand | P37468 |
Ligands and binding sites
- 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 | 1126 | 0.88 | 0.91 | 86 | empty |
| 2 | 1030 | 0.85 | 0.87 | 93 | empty |
| 3 | 990 | 0.83 | 0.85 | 63 | empty |
| 4 | 695 | 0.83 | 0.88 | 69 | empty |
| 5 | 600 | 0.83 | 0.89 | 71 | empty |
Interfaces
43 interfaces between chains.
- A–L · 3217 Ų buried · 73 hydrogen bonds · protein-nucleic
- A–D · 3129 Ų buried · 80 hydrogen bonds · protein-nucleic
- A–I · 3014 Ų buried · 66 hydrogen bonds · protein-nucleic
- A–Q · 2714 Ų buried · 49 hydrogen bonds · protein-nucleic
- A–T · 2585 Ų buried · 48 hydrogen bonds · protein-nucleic
Compared structures
- 7V2M · T.thermophilus 30S ribosome with KsgA, class K1k4 · the same entry in another collection · chain K against K, 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 P0DOY9
- 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 P0DOY6
- Every structure of UniProt Q5SJ76
- Every structure of UniProt Q5SJH3
- Every structure of UniProt P0DOY7
- Every structure of UniProt Q5SLQ0
- Every structure of UniProt Q5SHP2
- Every structure of UniProt P80380
- Every structure of UniProt P37468
- Every structure of UniProt Q5SIH3
- Elsewhere: RCSB PDB 7V2M · PDBe 7V2M · UniProt P80371 · UniProt P80372 · UniProt P80373 · UniProt Q5SHQ5 · UniProt Q5SLP8 · UniProt P17291 · UniProt P0DOY9 · UniProt P80374 · UniProt Q5SHN7 · UniProt P80376 · UniProt Q5SHN3 · UniProt P80377 · UniProt P0DOY6 · UniProt Q5SJ76 · UniProt Q5SJH3 · UniProt P0DOY7 · UniProt Q5SLQ0 · UniProt Q5SHP2 · UniProt P80380 · UniProt P37468 · UniProt Q5SIH3
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