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Crystal structure of human insulin with NI+2 complex

Analyse Crystal structure of human insulin with NI+2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3INC
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
NI

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CInsulin a chainprotein2167% helix, 10% strandP01308
B, DInsulin B chainprotein3037% helix, 13% strandP01308

Ligands and binding sites

  • NI · Nickel (II) 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.

  • A–B · 886 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 843 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 626 Ų buried · 7 hydrogen bonds · protein-protein
  • A–D · 70 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 63 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 3INC · Crystal structure of human insulin with Ni+2 complex · the same entry in another collection · chain A against A, TM-score 1.00

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