Research workbench
NMR structure of human insulin mutant gly-B20-D-ala, gly-B23-D-ala pro-B28-lys, lys-B29-pro, 20 structures
Analyse NMR structure of human insulin mutant gly-B20-D-ala, gly-B23-D-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
- 2L1Z
- Type
- protein
- Length
- 51 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin a chain; Insulin B chain
- UniProt
- P01308
Structure
solution nmr · 2 distinct chains · 45% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin a chain | protein | 21 | 52% helix, 10% strand | P01308 |
| B | Insulin B chain | protein | 30 | 40% helix, 7% strand | P01308 |
Interfaces
1 interface between chains.
- A–B · 686 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2L1Z · NMR Structure of human insulin mutant GLY-B20-D-ALA, GLY-B23-D-ALA PRO-B28-LYS… · 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 2L1Z · PDBe 2L1Z · UniProt P01308
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