Research workbench
Crystal structure of human insulin analogue (nme-ALAB8)- insulin crystal form II
Analyse Crystal structure of human insulin analogue (nme-ALAB8)- insulin crystal form II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CY7
- Type
- protein
- Length
- 100 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin a chain; Insulin B chain
- UniProt
- P01308
- Ligands
- SO4
Structure
x-ray diffraction · 3 distinct chains · 53% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin a chain | protein | 21 | 57% helix, 5% strand | P01308 |
| B | Insulin B chain | protein | 28 | 54% helix, 4% strand | P01308 |
| D | Insulin B chain | protein | 30 | 50% helix, 3% strand | P01308 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- C–D · 657 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 547 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 319 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 255 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 154 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 4CY7 · Crystal structure of human insulin analogue (NMe-AlaB8)-insulin crystal form II · 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 4CY7 · PDBe 4CY7 · UniProt P01308
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