MolNFT v1 · #184378 · protein + RNA
Mycoplasma pneumoniae 30S subunit of ribosomes in chloramphenicol- treated cells
7OOC: “Mycoplasma pneumoniae 30S subunit of ribosomes in chloramphenicol- treated cells”. Electron microscopy, 1 ligand (ZN). MolNFT v1 #184378 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7OOC
- Type
- protein + RNA
- Length
- 3,964 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P41205, Q50301, P75545, P75560, P75179, Q50296, P46775, P75237, A0A0H3DLS7, P75546, Q50305, P75581, Q50297, P75173, P75576, P57079, Q50304, P75541, P75543, Q50309
- Ligands
- ZN
Structure
electron microscopy · 21 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 215 | — | P41205 |
| D | — | protein | 153 | — | Q50301 |
| F | — | protein | 154 | — | P75545 |
| A | — | protein | 249 | — | P75560 |
| H | — | protein | 128 | — | P75179 |
| J | — | protein | 114 | — | Q50296 |
| C | — | protein | 203 | — | P46775 |
| S | — | protein | 77 | — | P75237 |
| O | — | protein | 87 | — | A0A0H3DLS7 |
| K | — | protein | 136 | — | P75546 |
| M | — | protein | 60 | — | Q50305 |
| I | — | protein | 101 | — | P75581 |
| L | — | protein | 118 | — | Q50297 |
| N | — | protein | 83 | — | P75173 |
| R | — | protein | 84 | — | P75576 |
| T | — | protein | 53 | — | P57079 |
| G | — | protein | 141 | — | Q50304 |
| Q | — | protein | 65 | — | P75541 |
| E | — | protein | 167 | — | P75543 |
| P | — | protein | 83 | — | Q50309 |
| 5 | — | rna | 1493 | — | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains M, Q
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7OOC · Mycoplasma pneumoniae 30S subunit of ribosomes in chloramphenicol-treated cells · the same entry in another collection · chain S against S, 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 P41205
- Every structure of UniProt Q50301
- Every structure of UniProt P75545
- Every structure of UniProt P75560
- Every structure of UniProt P75179
- Every structure of UniProt Q50296
- Every structure of UniProt P46775
- Every structure of UniProt P75237
- Every structure of UniProt A0A0H3DLS7
- Every structure of UniProt P75546
- Every structure of UniProt Q50305
- Every structure of UniProt P75581
- Every structure of UniProt Q50297
- Every structure of UniProt P75173
- Every structure of UniProt P75576
- Every structure of UniProt P57079
- Every structure of UniProt Q50304
- Every structure of UniProt P75541
- Every structure of UniProt P75543
- Every structure of UniProt Q50309
- Elsewhere: RCSB PDB 7OOC · PDBe 7OOC · UniProt P41205 · UniProt Q50301 · UniProt P75545 · UniProt P75560 · UniProt P75179 · UniProt Q50296 · UniProt P46775 · UniProt P75237 · UniProt A0A0H3DLS7 · UniProt P75546 · UniProt Q50305 · UniProt P75581 · UniProt Q50297 · UniProt P75173 · UniProt P75576 · UniProt P57079 · UniProt Q50304 · UniProt P75541 · UniProt P75543 · UniProt Q50309
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