MolNFT v1 · #17391 · protein
Dehydrated T6 human insulin at 100 K
1OS3: “Dehydrated T6 human insulin at 100 K”. X-ray diffraction, 2 ligands (ZN, CL). MolNFT v1 #17391 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OS3
- Type
- protein
- Length
- 99 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01308
- Ligands
- ZN, CL
Structure
x-ray diffraction · 3 distinct chains · 55% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin | protein | 21 | 67% helix, 10% strand | P01308 |
| B | Insulin | protein | 29 | 48% helix, 14% strand | P01308 |
| D | Insulin | protein | 28 | 54% helix, 14% strand | P01308 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- C–D · 904 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 812 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 544 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 61 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 48 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1OS3 · Dehydrated T6 human insulin at 100 K · the same entry in another collection · chain D against D, 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 1OS3 · PDBe 1OS3 · UniProt P01308
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