Research workbench
Structure of B28 asp insulin in complex with phenol
Analyse Structure of B28 asp insulin in complex with phenol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZEG
- Type
- protein
- Length
- 102 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01308
- Ligands
- IPH, ZN, CL
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin | protein | 21 | 62% helix, 5% strand | P01308 |
| B, D | Insulin | protein | 30 | 67% helix, 13% strand | P01308 |
Ligands and binding sites
- IPH · Phenol · ligand · 3 copies · chains A, B, D, C
- 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.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.32 | 0.75 | 17 | empty |
Interfaces
5 interfaces between chains.
- B–D · 701 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 660 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 630 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 66 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 15 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1ZEG · Structure of B28 asp insulin in complex with phenol · 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 1ZEG · PDBe 1ZEG · UniProt P01308
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