MolNFT v1 · #11576 · protein
Fitting of L11 protein and elongation factor G (domain G' and V) in the cryo-EM MAP of E. COLI 70S ribosome bound with ef-G and gmppcp, a nonhydrolysable GTP analog
1JQS · 50S ribosomal protein L11: “Fitting of L11 protein and elongation factor G (domain G' and V) in the cryo-EM MAP of E. COLI 70S ribosome…”. Electron microscopy. MolNFT v1 #11576 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1JQS
- Type
- protein
- Length
- 233 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 50S ribosomal protein L11; Elongation factor G
- UniProt
- P29395, P13551
Structure
electron microscopy · 3 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 50S ribosomal protein L11 | protein | 133 | 0% helix, 0% strand | P29395 |
| B | Elongation factor G | protein | 32 | 0% helix, 0% strand | P13551 |
| C | Elongation factor G | protein | 68 | 0% helix, 0% strand | P13551 |
Compared structures
- 1JQS · Fitting of L11 protein and elongation factor G (domain G' and V) in the cryo-em map of E.… · the same entry in another collection · chain A against A, TM-score 1.00
- P13551 · AlphaFold monomer V2.0 prediction for elongation factor G (P13551) · a predicted model of the same protein · chain C against A, TM-score 0.81
- 1OLN · Model for thiostrepton antibiotic binding to L11 substrate from 50S ribosomal RNA · a predicted model of the same protein · chain A against A, TM-score 0.80
- 1OLN · Model for thiostrepton antibiotic binding to L11 substrate from 50S ribosomal RNA · a predicted model of the same protein · chain A against A, TM-score 0.80
- P29395 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L11 (P29395) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 P29395
- Every structure of UniProt P13551
- Elsewhere: RCSB PDB 1JQS · PDBe 1JQS · UniProt P29395 · UniProt P13551
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