Research workbench
Ttslyd with W4A pseudo-wild-type S2 peptide
Analyse Ttslyd with W4A pseudo-wild-type S2 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OXI
- Type
- protein
- Length
- 175 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase; 30S ribosomal protein S2
- EC
- 5.2.1.8
- UniProt
- Q5SLE7, P0A7V0
- Ligands
- CL
Structure
x-ray diffraction · 3 distinct chains · 15% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 150 | 15% helix, 45% strand | Q5SLE7 |
| B | 30S ribosomal protein S2 | protein | 14 | 29% helix, 7% strand | P0A7V0 |
| C | 30S ribosomal protein S2 | protein | 11 | 0% helix, 9% strand | P0A7V0 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 846 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 658 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 40 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7OXI · ttSlyD with W4A pseudo-wild-type S2 peptide · the same entry in another collection · chain A against A, 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 Q5SLE7
- Every structure of UniProt P0A7V0
- Elsewhere: RCSB PDB 7OXI · PDBe 7OXI · UniProt Q5SLE7 · UniProt P0A7V0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.