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Design of an insulin analog with enhanced receptor-binding selectivity. Rationale, structure, and therapeutic implications

Analyse Design of an insulin analog with enhanced receptor-binding selectivity.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FQ9
Type: protein
Length: 102 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.35
Molecule: Insulin
UniProt: P01308
Ligands: ZN

Structure

x-ray diffraction · resolution 1.35 · 2 distinct chains · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Insulin	protein	21	67% helix, 10% strand	P01308
B, D	Insulin	protein	30	47% helix, 13% strand	P01308

Ligands and binding sites

ZN · Zinc 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.

C–D · 925 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 917 Å² buried · 14 hydrogen bonds · protein-protein
B–D · 616 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 65 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 50 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

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

Compared structures

3FQ9 · Design of an insulin analog with enhanced receptor-binding selectivity. rationale… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P01308
Elsewhere: RCSB PDB 3FQ9 · PDBe 3FQ9 · UniProt P01308

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