Research workbench
Insulin with proline analog dhp at position B28 in the R6 state
Analyse Insulin with proline analog dhp at position B28 in the R6 state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5URU
- Type
- protein
- Length
- 194 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin chain a; Insulin chain B
- UniProt
- P01308
- Ligands
- IPH, ZN, CL
Structure
x-ray diffraction · 3 distinct chains · 70% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Insulin chain a | protein | 21 | 57% helix, 5% strand | P01308 |
| B, H | Insulin chain B | protein | 28 | 75% helix, 11% strand | P01308 |
| D, F | Insulin chain B | protein | 27 | 74% helix, 11% strand | P01308 |
Ligands and binding sites
- IPH · Phenol · ligand · 4 copies · chains A, B, C, D, E, F, G, H
- ZN · Zinc ion · metal · 4 copies · chains B, D, F, H
- CL · Chloride ion · ion · 4 copies · chains B, D, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
10 interfaces between chains.
- B–D · 630 Ų buried · 9 hydrogen bonds · protein-protein
- F–H · 623 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 568 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 568 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 535 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 4 modified (disulfide, nonstandard).
Compared structures
- 5URU · Insulin with proline analog DhP at position B28 in the R6 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 5URU · PDBe 5URU · UniProt P01308
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