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Crystal structure of the B24HIS-insulin - human analogue

Analyse Crystal structure of the B24HIS-insulin - human analogue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZI3
Type
protein
Length
41 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin
UniProt
P01308
Ligands
SO4

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInsulinprotein2157% helix, 0% strandP01308
BInsulinprotein2055% helix, 0% strandP01308

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 456 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 3ZI3 · Crystal structure of the B24His-insulin - human analogue · the same entry in another collection · chain A against A, TM-score 1.00

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