Research workbench
In meso in situ serial X-ray crystallography structure of insulin at 100 K
Analyse In meso in situ serial X-ray crystallography structure of insulin at 100 K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5D53
- Type
- protein
- Length
- 51 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin B chain; Insulin a chain
- UniProt
- P01315
- Ligands
- PO4
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin B chain | protein | 21 | 57% helix, 5% strand | P01315 |
| B | Insulin a chain | protein | 30 | 47% helix, 3% strand | P01315 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains B
- PE5 · 3,6,9,12,15,18,21,24-octaoxahexacosan-1-ol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 776 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 5D53 · In meso in situ serial X-ray crystallography structure of insulin at 100 K · 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 P01315
- Elsewhere: RCSB PDB 5D53 · PDBe 5D53 · UniProt P01315
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