Research workbench
Insulin glulisine
Analyse Insulin glulisine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GV0
- Type
- protein
- Length
- 100 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01308
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G, I | Insulin | protein | 21 | 67% helix, 10% strand | P01308 |
| B, D | Insulin | protein | 29 | 52% helix, 14% strand | P01308 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B, D
- FMT · Formic acid · additive · 2 copies · chains I, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- G–B · 914 Ų buried · 15 hydrogen bonds · protein-protein
- I–D · 900 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 564 Ų buried · 8 hydrogen bonds · protein-protein
- G–D · 61 Ų buried · 0 hydrogen bonds · protein-protein
- B–I · 46 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6GV0 · Insulin glulisine · the same entry in another collection · chain G against G, 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 6GV0 · PDBe 6GV0 · UniProt P01308
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