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Insulin protein crystallization via langmuir-blodgett

Analyse Insulin protein crystallization via langmuir-blodgett in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4I5Y
Type: protein
Length: 51 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.8
Source: Bos taurus
Molecule: Insulin
UniProt: P01317

Structure

x-ray diffraction · resolution 1.8 · 2 distinct chains · 49% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Insulin	protein	21	52% helix, 5% strand	P01317
B	Insulin	protein	30	47% helix, 3% strand	P01317

Interfaces

1 interface between chains.

A–B · 793 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

4I5Y · Insulin protein crystallization via langmuir-blodgett · the same entry in another collection · chain A against A, TM-score 1.00
P01317 · AlphaFold monomer V2.0 prediction for insulin (P01317) · a predicted model of the same protein · chain B against A, TM-score 0.42

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 P01317
Elsewhere: RCSB PDB 4I5Y · PDBe 4I5Y · UniProt P01317

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