Research workbench
Insulin with proline analog pip at position B28 in the T2 state
Analyse Insulin with proline analog pip at position B28 in the T2 state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5USP
- Type
- protein
- Length
- 50 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin chain a; Insulin chain B
- UniProt
- P01308
- Ligands
- NA
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin chain a | protein | 21 | 48% helix, 5% strand | P01308 |
| B | Insulin chain B | protein | 29 | 48% helix, 3% strand | P01308 |
Ligands and binding sites
- NA · Sodium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 759 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 1 modified (disulfide, nonstandard).
Compared structures
- 5USP · Insulin with proline analog Pip at position B28 in the T2 state · 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 5USP · PDBe 5USP · UniProt P01308
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