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NMR structure of human insulin under amyloidogenic condition, 15 structures

Analyse NMR structure of human insulin under amyloidogenic condition, 15 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SF1
Type: protein
Length: 51 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin a chain; Insulin
UniProt: P01308
Pockets: 1 · best druggability 0.29

Structure

solution nmr · 2 distinct chains · 14% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Insulin a chain	protein	21	0% helix, 0% strand	P01308
B	Insulin	protein	30	23% helix, 0% strand	P01308

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.29	0.74	12	empty

Interfaces

1 interface between chains.

A–B · 421 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1SF1 · NMR STRUCTURE OF HUMAN INSULIN under Amyloidogenic Condition, 15 STRUCTURES · 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 1SF1 · PDBe 1SF1 · UniProt P01308

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