Research workbench
T6 human insulin at 1.0 a resolution
Analyse T6 human insulin at 1.0 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MSO
- Type
- protein
- Length
- 102 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin a-chain; Insulin B-chain
- UniProt
- P01308
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin a-chain | protein | 21 | 57% helix, 10% strand | P01308 |
| B, D | Insulin B-chain | protein | 30 | 47% helix, 13% strand | P01308 |
Ligands and binding sites
- ZN · Zinc 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.
- A–B · 872 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 830 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 633 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 56 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 53 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1MSO · T6 Human Insulin at 1.0 A Resolution · 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 P01308
- Elsewhere: RCSB PDB 1MSO · PDBe 1MSO · UniProt P01308
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