Research workbench
Des-B29,B30-insulin
Analyse Des-B29,B30-insulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JP3
- Type
- protein
- Length
- 294 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin B CHAIN,INSULIN a chain
- UniProt
- P01308
- Ligands
- IPH, ZN, CL
- Pockets
- 6 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Insulin B CHAIN,INSULIN a chain | protein | 49 | 67% helix, 8% strand | P01308 |
Ligands and binding sites
- IPH · Phenol · ligand · 6 copies · chains A, C, B, F, E, D
- ZN · Zinc ion · metal · 2 copies · chains A, C, E, B, D, F
- CL · Chloride ion · ion · 2 copies · chains B, D, F, A, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 562 | 0.80 | 0.86 | 76 | IPH |
| 2 | 187 | 0.69 | 0.87 | 30 | IPH |
| 3 | 281 | 0.68 | 0.83 | 48 | CL, IPH |
| 4 | 206 | 0.62 | 0.82 | 35 | IPH |
| 5 | 214 | 0.62 | 0.81 | 36 | IPH |
Interfaces
12 interfaces between chains.
- E–F · 768 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 762 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 698 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 296 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 281 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide (disulfide).
Compared structures
- 7JP3 · Des-B29,B30-insulin · 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 7JP3 · PDBe 7JP3 · UniProt P01308
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