Research workbench
Radiation damage study of Cu T6-insulin - 0.30 MGy
Analyse Radiation damage study of Cu T6-insulin - 0.30 MGy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M4J
- Type
- protein
- Length
- 100 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Bos taurus
- Molecule
- Insulin
- UniProt
- P01317
- Ligands
- CU
Structure
x-ray diffraction · resolution 1.9 · 3 distinct chains · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin | protein | 21 | 67% helix, 10% strand | P01317 |
| B | Insulin | protein | 28 | 50% helix, 14% strand | P01317 |
| D | Insulin | protein | 30 | 47% helix, 13% strand | P01317 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- C–D · 898 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 838 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 626 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 62 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 48 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 P01317
- Elsewhere: RCSB PDB 4M4J · PDBe 4M4J · UniProt P01317
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