MolNFT v1 · #121253 · protein
Insulin with proline analog hyp at position B28 in the T2 state
5HPR · Insulin a-chain: “Insulin with proline analog hyp at position B28 in the T2 state”. X-ray diffraction, 1 ligand (NA). MolNFT v1 #121253 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5HPR
- Type
- protein
- Length
- 51 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin a-chain; Insulin B-chain
- UniProt
- P01308
- Ligands
- NA
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin a-chain | protein | 21 | 48% helix, 5% strand | P01308 |
| B | Insulin B-chain | protein | 30 | 47% helix, 3% strand | P01308 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 816 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 1 modified (disulfide, hydroxylation).
Compared structures
- 5HPR · Insulin with proline analog HyP 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 5HPR · PDBe 5HPR · UniProt P01308
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