MolNFT v2 · #121581 · protein
Insulin with proline analog HyP at position B28 in the R6 state
5HPU: “Insulin with proline analog HyP at position B28 in the R6 state”. X-ray diffraction at 2.2, 3 ligands (IPH, ZN, CL). MolNFT v2 #121581 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5HPU
- Type
- protein
- Length
- 97 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Homo sapiens
- UniProt
- P01308
- Ligands
- IPH, ZN, CL
Structure
x-ray diffraction · resolution 2.2 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 21 | — | P01308 |
| B | — | protein | 27 | — | P01308 |
| D | — | protein | 28 | — | P01308 |
Ligands and binding sites
- IPH · Phenol · ligand · 2 copies · chains A, B, C, D
- 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.
Compared structures
- 5HPU · Insulin with proline analog hyp 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 5HPU · PDBe 5HPU · UniProt P01308
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