MolNFT v1 · #40319 · protein
The structure of des-phe B1 bovine insulin
2INS · Des-phe B1 insulin (chain a): “The structure of des-phe B1 bovine insulin”. X-ray diffraction, 1 ligand (ZN). MolNFT v1 #40319 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2INS
- Type
- protein
- Length
- 100 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Des-phe B1 insulin (chain a); Des-phe B1 insulin (chain B)
- UniProt
- P01317
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Des-phe B1 insulin (chain a) | protein | 21 | 67% helix, 10% strand | P01317 |
| B, D | Des-phe B1 insulin (chain B) | protein | 29 | 48% helix, 10% strand | P01317 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- C–D · 852 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 812 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 646 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 67 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 37 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 P01317
- Elsewhere: RCSB PDB 2INS · PDBe 2INS · UniProt P01317
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