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X-ray diffraction structure of bovine insulin at 2.3 a resolution

Analyse X-ray diffraction structure of bovine insulin at 2.3 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZI8
Type
protein
Length
99 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin
UniProt
P01317
Ligands
ZN, CL

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CInsulinprotein2157% helix, 10% strandP01317
BInsulinprotein2948% helix, 14% strandP01317
DInsulinprotein2850% helix, 14% strandP01317

Ligands and binding sites

  • 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 · 870 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 823 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 621 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 59 Ų buried · 1 hydrogen bond · protein-protein
  • A–D · 55 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 6ZI8 · X-ray diffraction structure of bovine insulin at 2.3 A resolution · the same entry in another collection · chain A against A, TM-score 1.00

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