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X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agents, thiocyanate, methylparaben and phenol

Analyse X-ray crystallographic studies on hexameric insulins in the presence of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2TCI
Type: protein
Length: 100 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thiocyanate insulin
UniProt: P01315
Ligands: ZN, SCN

Structure

x-ray diffraction · 3 distinct chains · 59% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Thiocyanate insulin	protein	21	62% helix, 5% strand	P01315
B	Thiocyanate insulin	protein	28	68% helix, 11% strand	P01315
D	Thiocyanate insulin	protein	30	50% helix, 10% strand	P01315

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains B, D
SCN · Thiocyanate ion · ion · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

5 interfaces between chains.

C–D · 805 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 662 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 585 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 62 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 36 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

2TCI · X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing… · 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 P01315
Elsewhere: RCSB PDB 2TCI · PDBe 2TCI · UniProt P01315

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