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Dehydrated T6 human insulin at 295 K

Analyse Dehydrated T6 human insulin at 295 K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OS4
Type: protein
Length: 294 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin
UniProt: P01308
Ligands: ZN
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 4 distinct chains · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, I, K	Insulin	protein	21	67% helix, 10% strand	P01308
B	Insulin	protein	29	52% helix, 14% strand	P01308
D, F, H, J, L	Insulin	protein	28	50% helix, 14% strand	P01308
G	Insulin	protein	20	55% helix, 10% strand	P01308

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains B, F, J, D, H, L

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	673	0.79	0.83	72	ZN

Interfaces

33 interfaces between chains.

K–L · 893 Å² buried · 9 hydrogen bonds · protein-protein
C–D · 888 Å² buried · 9 hydrogen bonds · protein-protein
G–H · 815 Å² buried · 10 hydrogen bonds · protein-protein
I–J · 787 Å² buried · 8 hydrogen bonds · protein-protein
E–F · 782 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

1OS4 · Dehydrated T6 human insulin at 295 K · 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 1OS4 · PDBe 1OS4 · UniProt P01308

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