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INSULIN'S biosynthesis and activity have opposing structural requirements: a new factor in neonatal diabetes mellitus

Analyse INSULIN'S biosynthesis and activity have opposing structural requirements: a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3JSD
Type
protein
Length
102 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
IPH, ZN, CL

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CInsulin a chainprotein2152% helix, 5% strandP01308
B, DInsulin B chainprotein3040% helix, 10% strandP01308

Ligands and binding sites

  • IPH · Phenol · ligand · chains C, D
  • ZN · Zinc ion · metal · 2 copies · chains B, D
  • CL · Chloride ion · ion · 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.

  • A–B · 882 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 625 Ų buried · 3 hydrogen bonds · protein-protein
  • B–D · 622 Ų buried · 9 hydrogen bonds · protein-protein
  • A–D · 60 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 28 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 d-amino (disulfide, D-amino acid).

Compared structures

  • 3JSD · Insulin's biosynthesis and activity have opposing structural requirements: a new factor… · the same entry in another collection · chain A against A, TM-score 1.00

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