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Crystal structure of allo-ILEA2-insulin, an inactive chiral analogue: implications for the mechanism of receptor

Analyse Crystal structure of allo-ILEA2-insulin, an inactive chiral analogue… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q4V
Type: protein
Length: 102 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin
Ligands: IPH, ZN

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Insulin	protein	21	48% helix, 5% strand	—
B, D	Insulin	protein	30	37% helix, 10% strand	—

Ligands and binding sites

IPH · Phenol · ligand · chains C, D
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.

A–B · 845 Å² buried · 11 hydrogen bonds · protein-protein
B–D · 678 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 638 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 54 Å² buried · 1 hydrogen bond · protein-protein
B–C · 26 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

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

Compared structures

1Q4V · Crystal structure of allo-ILEA2-insulin, an inactive chiral analogue: implications for… · 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
Elsewhere: RCSB PDB 1Q4V · PDBe 1Q4V

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