Research workbench
X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agents, thiocyanate, methylparaben and phenol
Analyse X-ray crystallographic studies on hexameric insulins in the presence of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MPJ
- Type
- protein
- Length
- 100 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenol insulin
- UniProt
- P01315
- Ligands
- IPH, ZN, CL
Structure
x-ray diffraction · 3 distinct chains · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Phenol insulin | protein | 21 | 67% helix, 5% strand | P01315 |
| B | Phenol insulin | protein | 28 | 68% helix, 11% strand | P01315 |
| D | Phenol insulin | protein | 30 | 47% helix, 10% strand | P01315 |
Ligands and binding sites
- IPH · Phenol · ligand · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains B, D
- CL · Chloride ion · ion · 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 · 833 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 674 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 581 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 71 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 31 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1MPJ · X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing… · 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 P01315
- Elsewhere: RCSB PDB 1MPJ · PDBe 1MPJ · UniProt P01315
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