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Insulin with proline analog pip at position B28 in the R6 state

Analyse Insulin with proline analog pip at position B28 in the R6 state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5USS
Type
protein
Length
97 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin chain a; Insulin chain B
UniProt
P01308
Ligands
IPH, ZN, CL

Structure

x-ray diffraction · 3 distinct chains · 68% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CInsulin chain aprotein2157% helix, 5% strandP01308
BInsulin chain Bprotein2774% helix, 11% strandP01308
DInsulin chain Bprotein2871% helix, 11% strandP01308

Ligands and binding sites

  • IPH · Phenol · ligand · 2 copies · chains A, B, 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.

  • B–D · 615 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 576 Ų buried · 5 hydrogen bonds · protein-protein
  • C–D · 544 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 62 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 31 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 modified (disulfide, nonstandard).

Compared structures

  • 5USS · Insulin with proline analog PiP at position B28 in the R6 state · the same entry in another collection · chain A against A, TM-score 1.00

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