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NMR structure of human insulin mutant his-B10-asp, val-B12-ala, pro- B28-lys, lys-B29-pro, 15 structures
Analyse NMR structure of human insulin mutant his-B10-asp, val-B12-ala, pro- B28-lys… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T1K
- Type
- protein
- Length
- 51 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01308
Structure
solution nmr · 2 distinct chains · 39% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin | protein | 21 | 43% helix, 5% strand | P01308 |
| B | Insulin | protein | 30 | 37% helix, 3% strand | P01308 |
Interfaces
1 interface between chains.
- A–B · 792 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1T1K · NMR structure of human insulin mutant his-B10-asp, val-B12-ala, pro-B28-lys, lys-B29-pro… · 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 1T1K · PDBe 1T1K · UniProt P01308
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