Research workbench
The molecular recognition of kink turn structure by the L7AE class of proteins
Analyse The molecular recognition of kink turn structure by the L7AE class of proteins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BW0
- Type
- protein + RNA
- Length
- 143 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hmkt-7; 50S ribosomal protein L7AE
- UniProt
- O29494
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hmkt-7 | rna | 26 | — | — |
| B | 50S ribosomal protein L7AE | protein | 117 | 47% helix, 16% strand | O29494 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 609 Ų buried · 18 hydrogen bonds · protein-nucleic
Compared structures
- 4BW0 · The molecular recognition of kink turn structure by the L7Ae class of proteins · the same entry in another collection · chain A against A, TM-score 1.00
- O29494 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L7AE (O29494) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 O29494
- Elsewhere: RCSB PDB 4BW0 · PDBe 4BW0 · UniProt O29494
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